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1.
World J Emerg Med ; 13(3): 189-195, 2022.
Artículo en Inglés | MEDLINE | ID: mdl-35646216

RESUMEN

BACKGROUND: To investigate the clinical effectiveness of a pneumatic compression device (PCD) combined with low-molecular-weight heparin (LMWH) for the prevention and treatment of deep vein thrombosis (DVT) in trauma patients. METHODS: This study retrospectively analyzed 286 patients with mild craniocerebral injury and clavicular fractures admitted to our department from January 2016 to February 2020. Patients treated with only LMWH served as the control group, and patients treated with a PCD combined with LMWH as the observation group. The incidence of DVT, postoperative changes in the visual analogue scale (VAS) score, and coagulation function were observed and compared between the two groups. Excluding the influence of other single factors, binary logistic regression analysis was used to evaluate the use of a PCD in the patient's postoperative coagulation function. RESULTS: After excluding 34 patients who did not meet the inclusion criteria, 252 patients were were included. The incidence of DVT in the observation group was significantly lower than that in the control group (5.6% vs. 15.1%, χ2=4.605, P<0.05). The postoperative VAS scores of the two groups were lower than those before surgery (P<0.05). The coagulation function of the observation group was significantly higher than that of the control group, with a better combined anticoagulant effect (P<0.05). There were no significant differences between the two groups in preoperative or postoperative Glasgow Coma Scale scores, intraoperative blood loss, postoperative infection rate, or length of hospital stay (P>0.05). According to logistic regression analysis, the postoperative risk of DVT in patients who received LMWH alone was 1.764 times that of patients who received LMWH+PCD (P<0.05). The area under the receiver operating characteristic (AUROC) curve of partial thromboplastin time (APTT) and platelet (PLT) were greater than 0.5, indicating that they were the influence indicators of adding PCD to prevent DVT. Excluding the influence of other variables, LMWH+PCD effectively improved the coagulation function of patients. CONCLUSIONS: Compared with LMWH alone, LMWH+PCD could improve blood rheology and coagulation function in patients with traumatic brain injury and clavicular fracture, reduce the incidence of DVT, shorten the length of hospital stay, and improve the clinical effectiveness of treatment.

3.
J Proteomics ; 173: 115-125, 2018 02 20.
Artículo en Inglés | MEDLINE | ID: mdl-29197581

RESUMEN

Molting is an essential biological process occurring multiple times throughout the life cycle of most Ecdysozoa. Molting fluids accumulate and function in the exuvial space during the molting process. In this study, we used liquid chromatography-tandem mass spectrometry to investigate the molting fluids to analyze the molecular mechanisms of molting in the silkworm, Bombyx mori. In total, 375 proteins were identified in molting fluids from the silkworm at 14-16h before pupation and eclosion, including 12 chitin metabolism-related enzymes, 35 serine proteases, 15 peptidases, and 38 protease inhibitors. Gene ontology analysis indicated that "catalytic" constitutes the most enriched function in the molting fluid. Gene expression patterns and bioinformatic analyses suggested that numerous enzymes are involved in the degradation of cuticle proteins and chitin. Protein-protein interaction network and activity analyses showed that protease inhibitors are involved in the regulation of multiple pathways in molting fluid. Additionally, many immune-related proteins may be involved in the immune defense during molting. These results provide a comprehensive proteomic insight into proteolytic enzymes and protease inhibitors in molting fluid, and will likely improve the current understanding of physiological processes in insect molting. BIOLOGICAL SIGNIFICANCE: Insect molting constitutes a dynamic physiological process. To better understand this process, we used LC-MS/MS to investigate the proteome of silkworm molting fluids and identified key proteins involved in silkworm molting. The biological processes of the old cuticle degradation pathway and immune defense response were analyzed in the proteome of silkworm molting fluid. We report that protease inhibitors serve as key factors in the regulation of the molting process. The proteomic results provide new insight into biological molting processes in insects.


Asunto(s)
Bombyx/química , Muda/fisiología , Proteoma/metabolismo , Proteómica/métodos , Animales , Bombyx/fisiología , Proteínas de Insectos/metabolismo , Péptido Hidrolasas , Inhibidores de Proteasas , Mapas de Interacción de Proteínas , Proteoma/fisiología
4.
Int J Biol Macromol ; 107(Pt B): 2334-2341, 2018 Feb.
Artículo en Inglés | MEDLINE | ID: mdl-29055702

RESUMEN

Invertase or ß-fructofuranosidase (EC 3.2.1.26) belongs to the glycoside hydrolase family 32, which catalyzes the hydrolysis of sucrose into fructose and glucose. Here, we report the biochemical and functional characterization of invertase Bmsuc1 from Bombyx mori. Bmsuc1 showed optimal hydrolysis at pH 7.0-8.0 and its optimum temperature is 50°C using sucrose as substrate. Circular dichroism spectra indicated Bmsuc1 had a primarily ß-strand structure. The thermal denaturations transition of Bmsuc1 was a cooperative process with a Tm, ΔH, and ΔS of 53.81±0.12°C, 185.51±0.14KJ/mol and 0.56±0.01KJ/(molK), respectively. Moreover, homology modeling and multi-sequence alignment suggested that Bmsuc1 has a canonical ß-propeller fold and one conserved catalytic triad, Asp63-Asp181-Glu234, which is located in the bottom of the substrate-binding pocket. Bmsuc1 was expressed at high levels in the silk gland at both the transcriptional and translational levels. These expression profiles combined with invertase activity analyses of Bmsuc1 suggested that it might function as a digestive enzyme to hydrolyze sugar in the silk gland lumen. Collectively, these findings expand towards a better understanding of the structure of Bmsuc1 and its function in the silk gland.


Asunto(s)
Bombyx/enzimología , Estructura Secundaria de Proteína , beta-Fructofuranosidasa/química , Secuencia de Aminoácidos/genética , Animales , Bombyx/genética , Clonación Molecular , Fructosa/química , Hidrólisis , Simulación de Dinámica Molecular , Relación Estructura-Actividad , Sacarosa/química , beta-Fructofuranosidasa/genética , beta-Fructofuranosidasa/metabolismo
5.
Insect Sci ; 24(5): 753-767, 2017 Oct.
Artículo en Inglés | MEDLINE | ID: mdl-27311916

RESUMEN

Serine proteases play important roles in digestion and immune responses during insect development. In the present study, the serine protease gene BmSP36, which encodes a 292-residue protein, was cloned from the midgut cells of Bombyx mori. BmSP36 contains an intact catalytic triad (H57, D102 and S195) and a conserved substrate-binding site (G189, H216 and G226), suggesting that it is a serine protease with chymotrypsin-like specificity. The temporal and spatial expression patterns of BmSP36 indicated that its messenger RNA and protein expression mainly occurred in the midgut at the feeding stages. Western blotting, immunofluorescence and liquid chromatography-tandem mass spectrometry analyses revealed secretion of BmSP36 protein from epithelial cells into the midgut lumen. The transcriptional and translational expression of BmSP36 was down-regulated after starvation but up-regulated after refeeding. Moreover, expression of the BmSP36 gene could be up-regulated by a juvenile hormone analogue. These results enable us to better define the potential role of BmSP36 in dietary protein digestion at the feeding stages during larval development.


Asunto(s)
Bombyx/enzimología , Proteínas de Insectos/metabolismo , Serina Proteasas/metabolismo , Secuencia de Aminoácidos , Animales , Western Blotting , Proteínas en la Dieta/metabolismo , Digestión , Técnica del Anticuerpo Fluorescente , Privación de Alimentos , Tracto Gastrointestinal/enzimología , Regulación de la Expresión Génica , Hormonas Juveniles , Larva/enzimología , Pupa/enzimología , Reacción en Cadena en Tiempo Real de la Polimerasa
6.
Sci Rep ; 5: 11863, 2015 Jul 07.
Artículo en Inglés | MEDLINE | ID: mdl-26148664

RESUMEN

Serpins generally serve as inhibitors that utilize a mobile reactive center loop (RCL) as bait to trap protease targets. Here, we present the crystal structure of serpin18 from Bombyx mori at 1.65 Å resolution, which has a very short and stable RCL. Activity analysis showed that the inhibitory target of serpin18 is a cysteine protease rather than a serine protease. Notably, this inhibitiory reaction results from the formation of an intermediate complex, which then follows for the digestion of protease and inhibitor into small fragments. This activity differs from previously reported modes of inhibition for serpins. Our findings have thus provided novel structural insights into the unique inhibitory mechanism of serpin18. Furthermore, one physiological target of serpin18, fibroinase, was identified, which enables us to better define the potential role for serpin18 in regulating fibroinase activity during B. mori development.


Asunto(s)
Bombyx/metabolismo , Proteínas de Insectos/química , Inhibidores de Proteasas/química , Serpinas/química , Secuencia de Aminoácidos , Animales , Cristalografía por Rayos X , Electroforesis en Gel de Poliacrilamida , Humanos , Proteínas de Insectos/genética , Proteínas de Insectos/metabolismo , Cinética , Datos de Secuencia Molecular , Inhibidores de Proteasas/metabolismo , Estructura Terciaria de Proteína , Proteínas Recombinantes/biosíntesis , Proteínas Recombinantes/química , Proteínas Recombinantes/aislamiento & purificación , Alineación de Secuencia , Serina Endopeptidasas/química , Serpinas/genética , Serpinas/metabolismo
7.
Biochem Biophys Res Commun ; 457(1): 31-6, 2015 Jan 30.
Artículo en Inglés | MEDLINE | ID: mdl-25529451

RESUMEN

Serpins (serine proteinase inhibitors) are widely distributed in different species and are well known for their inhibitory activities towards serine proteinases. Here, we report the functional characterization of Bombyx mori serpin16. Expression analysis showed that serpin16 was specifically expressed at high levels in the silk gland at both the transcriptional and translational levels. Moreover, homology modeling and multi-sequence alignment suggested that serpin16 had a canonical serpin fold, but it contained a unique reactive center loop, which was obviously shorter than that of typical serpins. Inhibitory activity analyses revealed that the target proteinase of serpin18 is a cysteine proteinase, rather than a serine proteinase. Furthermore, a Michaelis complex model of serpin16 with its target proteinase was constructed to explain the structural basis of how serpin16 recognizes the cysteine proteinase and its target specificity.


Asunto(s)
Estructuras Animales/metabolismo , Bombyx/metabolismo , Proteasas de Cisteína/metabolismo , Especificidad de Órganos , Inhibidores de Proteasas/metabolismo , Seda/metabolismo , Secuencia de Aminoácidos , Animales , Regulación de la Expresión Génica , Proteínas de Insectos/metabolismo , Modelos Moleculares , Datos de Secuencia Molecular , Inhibidores de Proteasas/química , Análisis de Secuencia de Proteína , Especificidad por Sustrato
8.
Biochim Biophys Acta ; 1844(9): 1486-92, 2014 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-24879127

RESUMEN

Saccharomyces cerevisiae Gre2 (EC1.1.1.283) serves as a versatile enzyme that catalyzes the stereoselective reduction of a broad range of substrates including aliphatic and aromatic ketones, diketones, as well as aldehydes, using NADPH as the cofactor. Here we present the crystal structures of Gre2 from S. cerevisiae in an apo-form at 2.00Å and NADPH-complexed form at 2.40Å resolution. Gre2 forms a homodimer, each subunit of which contains an N-terminal Rossmann-fold domain and a variable C-terminal domain, which participates in substrate recognition. The induced fit upon binding to the cofactor NADPH makes the two domains shift toward each other, producing an interdomain cleft that better fits the substrate. Computational simulation combined with site-directed mutagenesis and enzymatic activity analysis enabled us to define a potential substrate-binding pocket that determines the stringent substrate stereoselectivity for catalysis.


Asunto(s)
Apoenzimas/química , Coenzimas/química , NADP/química , Oxidorreductasas/química , Subunidades de Proteína/química , Proteínas de Saccharomyces cerevisiae/química , Saccharomyces cerevisiae/química , Secuencia de Aminoácidos , Apoenzimas/genética , Apoenzimas/metabolismo , Coenzimas/metabolismo , Cristalografía por Rayos X , Cinética , Simulación del Acoplamiento Molecular , Datos de Secuencia Molecular , Mutagénesis Sitio-Dirigida , NADP/metabolismo , Oxidorreductasas/genética , Oxidorreductasas/metabolismo , Unión Proteica , Multimerización de Proteína , Subunidades de Proteína/genética , Subunidades de Proteína/metabolismo , Proteínas Recombinantes/química , Proteínas Recombinantes/genética , Proteínas Recombinantes/metabolismo , Saccharomyces cerevisiae/enzimología , Proteínas de Saccharomyces cerevisiae/genética , Proteínas de Saccharomyces cerevisiae/metabolismo , Alineación de Secuencia , Especificidad por Sustrato , Termodinámica
9.
Artículo en Inglés | MEDLINE | ID: mdl-24192347

RESUMEN

The primary role of yeast Ara1, previously mis-annotated as a D-arabinose dehydrogenase, is to catalyze the reduction of a variety of toxic α,ß-dicarbonyl compounds using NADPH as a cofactor at physiological pH levels. Here, crystal structures of Ara1 in apo and NADPH-complexed forms are presented at 2.10 and 2.00 Šresolution, respectively. Ara1 exists as a homodimer, each subunit of which adopts an (α/ß)8-barrel structure and has a highly conserved cofactor-binding pocket. Structural comparison revealed that induced fit upon NADPH binding yielded an intact active-site pocket that recognizes the substrate. Moreover, the crystal structures combined with computational simulation defined an open substrate-binding site to accommodate various substrates that possess a dicarbonyl group.


Asunto(s)
NADP/metabolismo , Oxidorreductasas Actuantes sobre Donantes de Grupos Aldehído u Oxo/química , Oxidorreductasas Actuantes sobre Donantes de Grupos Aldehído u Oxo/metabolismo , Proteínas de Saccharomyces cerevisiae/química , Proteínas de Saccharomyces cerevisiae/metabolismo , Saccharomyces cerevisiae/enzimología , Deshidrogenasas del Alcohol de Azúcar/química , Deshidrogenasas del Alcohol de Azúcar/metabolismo , Secuencia de Aminoácidos , Sitios de Unión , Biocatálisis , Cristalografía por Rayos X , Modelos Moleculares , Datos de Secuencia Molecular , Multimerización de Proteína , Alineación de Secuencia , Especificidad por Sustrato
10.
J Biol Chem ; 287(42): 34961-34969, 2012 Oct 12.
Artículo en Inglés | MEDLINE | ID: mdl-22910915

RESUMEN

The disulfide relay system in the mitochondrial intermembrane space drives the import of proteins with twin CX(9)C or twin CX(3)C motifs by an oxidative folding mechanism. This process requires disulfide bond transfer from oxidized Mia40 to a substrate protein. Reduced Mia40 is reoxidized/regenerated by the FAD-linked sulfhydryl oxidase Erv1 (EC 1.8.3.2). Full-length Erv1 consists of a flexible N-terminal shuttle domain (NTD) and a conserved C-terminal core domain (CTD). Here, we present crystal structures at 2.0 Å resolution of the CTD and at 3.0 Å resolution of a C30S/C133S double mutant of full-length Erv1 (Erv1FL). Similar to previous homologous structures, the CTD exists as a homodimer, with each subunit consisting of a conserved four-helix bundle that accommodates the isoalloxazine ring of FAD and an additional single-turn helix. The structure of Erv1FL enabled us to identify, for the first time, the three-dimensional structure of the Erv1NTD, which is an amphipathic helix flanked by two flexible loops. This structure also represents an intermediate state of electron transfer from the NTD to the CTD of another subunit. Comparative structural analysis revealed that the four-helix bundle of the CTD forms a wide platform for the electron donor NTD. Moreover, computational simulation combined with multiple-sequence alignment suggested that the amphipathic helix close to the shuttle redox enter is critical for the recognition of Mia40, the upstream electron donor. These findings provide structural insights into electron transfer from Mia40 via the shuttle domain of one subunit of Erv1 to the CTD of another Erv1 subunit.


Asunto(s)
Mitocondrias/enzimología , Proteínas Mitocondriales/química , Oxidorreductasas actuantes sobre Donantes de Grupos Sulfuro/química , Proteínas de Saccharomyces cerevisiae/química , Saccharomyces cerevisiae/enzimología , Secuencias de Aminoácidos , Sustitución de Aminoácidos , Cristalografía por Rayos X , Disulfuros/química , Disulfuros/metabolismo , Transporte de Electrón/fisiología , Mitocondrias/genética , Proteínas de Transporte de Membrana Mitocondrial/química , Proteínas de Transporte de Membrana Mitocondrial/genética , Proteínas de Transporte de Membrana Mitocondrial/metabolismo , Proteínas del Complejo de Importación de Proteínas Precursoras Mitocondriales , Proteínas Mitocondriales/genética , Proteínas Mitocondriales/metabolismo , Mutación Missense , Oxidorreductasas actuantes sobre Donantes de Grupos Sulfuro/genética , Oxidorreductasas actuantes sobre Donantes de Grupos Sulfuro/metabolismo , Pliegue de Proteína , Estructura Terciaria de Proteína , Saccharomyces cerevisiae/genética , Proteínas de Saccharomyces cerevisiae/genética , Proteínas de Saccharomyces cerevisiae/metabolismo
11.
J Mol Biol ; 412(2): 204-11, 2011 Sep 16.
Artículo en Inglés | MEDLINE | ID: mdl-21816159

RESUMEN

Glutathione transferases (GSTs) are ubiquitous detoxification enzymes that conjugate hydrophobic xenobiotics with reduced glutathione. The silkworm Bombyx mori encodes four isoforms of GST Omega (GSTO), featured with a catalytic cysteine, except that bmGSTO3-3 has an asparagine substitution of this catalytic residue. Here, we determined the 2.20-Å crystal structure of bmGSTO3-3, which shares a typical GST overall structure. However, the extended C-terminal segment that exists in all the four bmGSTOs occupies the G-site of bmGSTO3-3 and makes it unworkable, as shown by the activity assays. Upon mutation of Asn29 to Cys and truncation of the C-terminal segment, the in vitro GST activity of bmGSTO3-3 could be restored. These findings provided structural insights into the activity regulation of GSTOs.


Asunto(s)
Glutatión Transferasa/metabolismo , Secuencia de Aminoácidos , Animales , Glutatión Transferasa/química , Modelos Moleculares , Datos de Secuencia Molecular , Conformación Proteica , Homología de Secuencia de Aminoácido
12.
J Struct Biol ; 176(1): 112-8, 2011 Oct.
Artículo en Inglés | MEDLINE | ID: mdl-21820057

RESUMEN

Quinone oxidoreductase (QOR EC1.6.5.5) catalyzes the reduction of quinone to hydroxyquinone using NADPH as a cofactor. Here we present the crystal structure of the ζ-crystallin-like QOR Zta1 from Saccharomycescerevisiae in apo-form at 2.00 Šand complexed with NADPH at 1.59 Šresolution. Zta1 forms a homodimer, with each subunit containing a catalytic and a cofactor-binding domain. Upon NADPH binding to the interdomain cleft, the two domains shift towards each other, producing a better fit for NADPH, and tightening substrate binding. Computational simulation combined with site-directed mutagenesis and enzymatic activity analysis defined a potential quinone-binding site that determines the stringent substrate specificity. Moreover, multiple-sequence alignment and kinetics assays implied that a single-residue change from Arg in lower organisms to Gly in vertebrates possibly resulted in elevation of enzymatic activity of ζ-crystallin-like QORs throughout evolution.


Asunto(s)
Quinona Reductasas/química , Proteínas Recombinantes/química , Proteínas de Saccharomyces cerevisiae/química , Saccharomyces cerevisiae/enzimología , Secuencias de Aminoácidos , Secuencia de Aminoácidos , Sitios de Unión , Dominio Catalítico , Coenzimas , Simulación por Computador , Secuencia Conservada , Cristalografía por Rayos X , Pruebas de Enzimas , Enlace de Hidrógeno , Interacciones Hidrofóbicas e Hidrofílicas , Modelos Moleculares , Datos de Secuencia Molecular , Mutagénesis Sitio-Dirigida , Mutación Missense , NADP/química , Unión Proteica , Quinona Reductasas/genética , Quinonas/química , Proteínas Recombinantes/genética , Proteínas de Saccharomyces cerevisiae/genética
13.
J Struct Biol ; 175(3): 469-74, 2011 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-21600990

RESUMEN

The yeast Saccharomyces cerevisiae mitochondrial matrix factor Mmf1, a member in the YER057c/Yigf/Uk114 family, participates in isoleucine biosynthesis and mitochondria maintenance. Mmf1 physically interacts with another mitochondrial matrix protein Mam33, which is involved in the sorting of cytochrome b2 to the intermembrane space as well as mitochondrial ribosomal protein synthesis. To elucidate the structural basis for their interaction, we determined the crystal structures of Mmf1 and Mam33 at 1.74 and 2.10 Å, respectively. Both Mmf1 and Mam33 adopt a trimeric structure: each subunit of Mmf1 displays a chorismate mutase fold with a six-stranded ß-sheet flanked by two α-helices on one side, whereas a subunit of Mam33 consists of a twisted six-stranded ß-sheet surrounded by five α-helices. Biochemical assays combined with structure-based computational simulation enable us to model a putative complex of Mmf1-Mam33, which consists of one Mam33 trimer and two tandem Mmf1 trimers in a head-to-tail manner. The two interfaces between the ring-like trimers are mainly composed of electrostatic interactions mediated by complementary negatively and positively charged patches. These results provided the structural insights into the putative function of Mmf1 during mitochondrial protein synthesis via Mam33, a protein binding to mitochondrial ribosomal proteins.


Asunto(s)
Cristalografía por Rayos X/métodos , Proteínas Mitocondriales/química , Proteínas de Saccharomyces cerevisiae/química , Secuencia de Aminoácidos , Datos de Secuencia Molecular , Unión Proteica , Estructura Secundaria de Proteína , Homología de Secuencia de Aminoácido
14.
J Biol Chem ; 286(15): 13430-7, 2011 Apr 15.
Artículo en Inglés | MEDLINE | ID: mdl-21345799

RESUMEN

The methionine S-sulfoxide reductase MsrA catalyzes the reduction of methionine sulfoxide, a ubiquitous reaction depending on the thioredoxin system. To investigate interactions between MsrA and thioredoxin (Trx), we determined the crystal structures of yeast MsrA/Mxr1 in their reduced, oxidized, and Trx2-complexed forms, at 2.03, 1.90, and 2.70 Å, respectively. Comparative structure analysis revealed significant conformational changes of the three loops, which form a plastic "cushion" to harbor the electron donor Trx2. The flexible C-terminal loop enabled Mxr1 to access the methionine sulfoxide on various protein substrates. Moreover, the plasticity of the Trx binding site on Mxr1 provides structural insights into the recognition of diverse substrates by a universal catalytic motif of Trx.


Asunto(s)
Metionina Sulfóxido Reductasas/química , Oxidorreductasas/química , Proteínas de Saccharomyces cerevisiae/química , Saccharomyces cerevisiae/enzimología , Tiorredoxinas/química , Secuencias de Aminoácidos , Metionina/análogos & derivados , Metionina/química , Metionina/metabolismo , Metionina Sulfóxido Reductasas/metabolismo , Oxidorreductasas/metabolismo , Estructura Cuaternaria de Proteína , Proteínas de Saccharomyces cerevisiae/metabolismo , Relación Estructura-Actividad , Especificidad por Sustrato , Tiorredoxinas/metabolismo
15.
Acta Crystallogr Sect F Struct Biol Cryst Commun ; 66(Pt 12): 1557-61, 2010 Dec 01.
Artículo en Inglés | MEDLINE | ID: mdl-21139195

RESUMEN

Saccharomyces cerevisiae Hsp33/YOR391Cp is a member of the ThiI/DJ-1/PfpI superfamily. Hsp33 was overexpressed in Escherichia coli and its crystal structure was determined at 2.40 Šresolution. Structural comparison revealed that Hsp33 adopts an α/ß-hydrolase fold and possesses the putative Cys-His-Glu catalytic triad common to the Hsp31 family, suggesting that Hsp33 and Hsp31 share similar aminopeptidase activity, while structural deviations in helices α2-α3 of the core domain might be responsible for the access of different peptide substrates.


Asunto(s)
Aminopeptidasas/química , Proteínas de Saccharomyces cerevisiae/química , Saccharomyces cerevisiae/química , Secuencia de Aminoácidos , Dominio Catalítico , Cristalografía por Rayos X , Proteínas de Choque Térmico/química , Modelos Moleculares , Datos de Secuencia Molecular , Multimerización de Proteína , Estructura Secundaria de Proteína , Alineación de Secuencia , Homología Estructural de Proteína
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