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( Jun Sen Tong ),( Hui Seon Yang ),( Young Jun Im ) 전남대학교 약품개발연구소 2014 약품개발연구지 Vol.23 No.-
Guanylate kinase-associated protein (GKAP) is a scaffolding protein that plays a role in protein-protein interactions at the synaptic junction such as linking the NMDA receptor-PSD-95 complex to the Shank-Homer complex. In this study, the C-terminal helical domain of GKAP from Rattus norvegicus was purified and crystallized by the vapour-diffusion method. To improve the diffraction quality of the GKAP crystals, a flexible loop in GKAP was truncated and an MBP (maltose-binding protein)-GKAP fusion was constructed in which the last Cterminal helix of MBP is fused to the N-terminus of the GKAP domain. The MBP-GKAP crystals diffracted to 2.0 A resolution using synchrotron radiation. The crystal was orthorhombic, belonging to space group P21212, with unit-cell parameters a = 99.1, b = 158.7, c = 65.5 A. The Matthews coefficient was determined to be 2.44;``3 Da-1 (solvent content 49.5%) with two molecules in the asymmetric unit. Initial attempts to solve the structure by molecular replacement using the MBP structure were successful.
ELSEVIER : Structure of the GH1 domain of guanylate kinase-associated protein from Rattus norvegicus
( Jun Sen Tong ),( Hui Seon Yang ),( Soo Hyun Eom ),( Chang Ju Chun ),( Young Jun Im ) 전남대학교 약품개발연구소 2014 약품개발연구지 Vol.23 No.-
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 GHl domain of GKAP from Rattus norvegicus was determined in fusion with an N-terminal maltose-binding protein at 2.0 A resolution. The structure of GKAP GHl displays a three-helix bundle connected by short flexible loops. The predicted helix ot4 which was not visible in the crystal structure associates weakly with the helix ot3 suggesting dynamic nature of the GHl domain. The strict conservation of GHl domain across GKAP family members and the lack of a catalytic active site required for enzyme activity imply that the GHl domain might serve as a protein-protein interaction module for the synaptic protein clustering. ⓒ 2014 Elsevier Inc. All rights reserved.