ABSTRACT
Dynamic electrocardiography (DCG) or Holter is the best device to detect arrhythmia and can help early detection of some sudden cardiac death risk factors. The acquisition and recording system of the DCG, however, affects the data quality and the patients' comfort directly. This paper reviews the related latest studies, and discusses the importance of new ECG electrode and wireless dynamic monitoring in DCG monitoring field. Moreover, the existed main problems are summarized and classified and the prospects for the development trend are presented.
Subject(s)
Electrocardiography, Ambulatory/instrumentation , Electrocardiography, Ambulatory/trends , Electrodes , Humans , Wireless TechnologyABSTRACT
The Ca(2+)-dependent cysteine protease calpain along with its endogenous inhibitor calpastatin is widely distributed. The interactions between calpain and calpastatin have been studied to better understand the nature of calpain inhibition by calpastatin, which can aid the design of small molecule inhibitors to calpain. Here we present the crystal structure of a complex between a calpastatin peptide and the calcium-binding domain VI of calpain. DIC19 is a 19 residue peptide, which corresponds to one of the three interacting domains of calpastatin, which is known to interact with domain VI of calpain. We present two crystal structures of DIC19 bound to domain VI of calpain, determined by molecular replacement methods to 2.5A and 2.2A resolution. In the process of crystallizing the inhibitor complex, a new native crystal form was identified which had the homodimer 2-fold axis along a crystallographic axis as opposed to the previously observed dimer in the asymmetric unit. The crystal structures of the native domain VI and its inhibitor PD150606 (3-(4-iodophenyl)-2-mercapto-(Z)-2-propenoic acid) complex were determined with the help of molecular replacement methods to 2.0A and 2.3A resolution, respectively. In addition, we built a homology model for the complex between domain IV and DIA19 peptide of calpastatin. Finally, we present a model for the calpastatin-inhibited calpain.
Subject(s)
Calcium-Binding Proteins/chemistry , Calcium-Binding Proteins/metabolism , Calpain/antagonists & inhibitors , Calpain/chemistry , Models, Molecular , Acrylates/chemistry , Acrylates/metabolism , Acrylates/pharmacology , Amino Acid Sequence , Binding Sites , Calcium-Binding Proteins/pharmacology , Calpain/metabolism , Crystallography, X-Ray , Cysteine Proteinase Inhibitors/chemistry , Cysteine Proteinase Inhibitors/metabolism , Cysteine Proteinase Inhibitors/pharmacology , Molecular Sequence Data , Protein Conformation , Protein Structure, TertiaryABSTRACT
Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of the CAP-Gly domain of Caenorhabditis elegans F53F4.3 protein, solved by single wavelength sulfur-anomalous phasing, revealed a novel protein fold containing three beta-sheets. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove. Residues in the groove are highly conserved as measured from the information content of the aligned sequences. The C-terminal tail of another molecule in the crystal is bound in this groove.
