K83 site affects PICK1 PDZ binding ability / 浙江大学学报·医学版
Journal of Zhejiang University. Medical sciences
;
(6): 153-158, 2012.
Artigo
em Chinês
| WPRIM
| ID: wpr-247168
ABSTRACT
<p><b>OBJECTIVE</b>To investigate the role of 83 site in interaction of GluR2 C-terminal and PICK1 PDZ domain.</p><p><b>METHODS</b>Docking structure of PICK1 PDZ domain with GluR2 C terminal PDZ binding motif was built with computer software. After K83 site was substituted by other amino acid, the structure and binding energy were recalculated; meanwhile, site specific mutants were constructed using wild type full length cDNA as template. Mutants were co-transfected with GluR2 into HEK293T cells. After staining, the distribution of PICK1 and GluR2 were observed under confocal microscope.</p><p><b>RESULTS</b>Wild type PICK1 and GluR2 formed many co-clusters in HEK293T cells as reported by other research groups; but different K83 mutant had different distribution in HEK293T cells.</p><p><b>CONCLUSION</b>The K83 site in PDZ domain of PICK1 is important for the interaction between PICK1 and GluR2. Altering lysine will probably change the hydrophobic interactions, the hydrogen bonds or the electrostatic interactions formed between PICK1 PDZ domain and GluR2 C terminal; accordingly, that will change the binding capacity between PICK1 and GluR2 in varying degrees.</p>
Texto completo:
DisponíveL
Índice:
WPRIM (Pacífico Ocidental)
Assunto principal:
Ligação Proteica
/
Sítios de Ligação
/
Simulação por Computador
/
Proteínas Nucleares
/
Proteínas de Transporte
/
Química
/
Receptores de AMPA
/
Domínios PDZ
/
Células HEK293
/
Metabolismo
Limite:
Humanos
Idioma:
Chinês
Revista:
Journal of Zhejiang University. Medical sciences
Ano de publicação:
2012
Tipo de documento:
Artigo
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