期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 452, 期 1, 页码 130-135出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2014.08.073
关键词
Protein structure; X-ray crystallography; Synaptic scaffolding protein; GKAP; Protein-protein interaction; Helix bundle
资金
- National Research Foundation of Korea (NRF) - Ministry of Science, ICT and Future Planning [NRF-2011-0025110]
Guanylate-kinase-associated protein (GKAP) is a scaffolding protein that links NMDA receptor-PSD-95 to Shank-Homer complexes by protein-protein interactions at the synaptic junction. GKAP family proteins are characterized by the presence of a C-terminal conserved GKAP homology domain 1 (GH1) of unknown structure and function. In this study, crystal structure of the GH1 domain of GKAP from Rattus norvegicus was determined in fusion with an N-terminal maltose-binding protein at 2.0 angstrom resolution. The structure of GKAP GH1 displays a three-helix bundle connected by short flexible loops. The predicted helix alpha 4 which was not visible in the crystal structure associates weakly with the helix alpha 3 suggesting dynamic nature of the GH1 domain. The strict conservation of GH1 domain across GKAP family members and the lack of a catalytic active site required for enzyme activity imply that the GH1 domain might serve as a protein-protein interaction module for the synaptic protein clustering. (C) 2014 Elsevier Inc. All rights reserved.
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