K83 site affects PICK1 PDZ binding ability.
- Author:
Yong FENG
1
;
Mu QIAO
;
Yu-ting LU
;
Ya-jian JIANG
;
Na WANG
;
Li-jun ZHU
Author Information
- Publication Type:Journal Article
- MeSH: Binding Sites; Carrier Proteins; chemistry; metabolism; Computer Simulation; HEK293 Cells; Humans; Nuclear Proteins; chemistry; metabolism; PDZ Domains; Protein Binding; Receptors, AMPA; metabolism
- From: Journal of Zhejiang University. Medical sciences 2012;41(2):153-158
- CountryChina
- Language:Chinese
-
Abstract:
OBJECTIVETo investigate the role of 83 site in interaction of GluR2 C-terminal and PICK1 PDZ domain.
METHODSDocking 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.
RESULTSWild 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.
CONCLUSIONThe 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.
