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Title: Structure of the GH1 domain of guanylate kinase-associated protein from Rattus norvegicus

Abstract

Graphical abstract: - Highlights: • The crystal structure of GKAP homology domain 1 (GH1) was determined. • GKAP GH1 is a three-helix bundle connected by short flexible loops. • The predicted helix α4 associates weakly with the helix α3, suggesting dynamic nature of the GH1 domain. - Abstract: 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 Å resolution. The structure of GKAP GH1 displays a three-helix bundle connected by short flexible loops. The predicted helix α4 which was not visible in the crystal structure associates weakly with the helix α3 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.

Authors:
;  [1];  [2];  [1];  [1]
  1. College of Pharmacy, Chonnam National University, Gwangju 500-757 (Korea, Republic of)
  2. School of Life Sciences, Steitz Center for Structural Biology, and Department of Chemistry, Gwangju Institute of Science and Technology, Gwangju 500-712 (Korea, Republic of)
Publication Date:
OSTI Identifier:
22416741
Resource Type:
Journal Article
Journal Name:
Biochemical and Biophysical Research Communications
Additional Journal Information:
Journal Volume: 452; Journal Issue: 1; Other Information: Copyright (c) 2014 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0006-291X
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; CRYSTAL STRUCTURE; ENZYME ACTIVITY; JOINTS; MALTOSE; PHOSPHOTRANSFERASES; PROTEIN STRUCTURE; RECEPTORS; RESOLUTION; X RADIATION

Citation Formats

Tong, Junsen, Yang, Huiseon, Eom, Soo Hyun, Chun, ChangJu, E-mail: cchun1130@jnu.ac.kr, and Im, Young Jun, E-mail: imyoungjun@jnu.ac.kr. Structure of the GH1 domain of guanylate kinase-associated protein from Rattus norvegicus. United States: N. p., 2014. Web. doi:10.1016/J.BBRC.2014.08.073.
Tong, Junsen, Yang, Huiseon, Eom, Soo Hyun, Chun, ChangJu, E-mail: cchun1130@jnu.ac.kr, & Im, Young Jun, E-mail: imyoungjun@jnu.ac.kr. Structure of the GH1 domain of guanylate kinase-associated protein from Rattus norvegicus. United States. doi:10.1016/J.BBRC.2014.08.073.
Tong, Junsen, Yang, Huiseon, Eom, Soo Hyun, Chun, ChangJu, E-mail: cchun1130@jnu.ac.kr, and Im, Young Jun, E-mail: imyoungjun@jnu.ac.kr. Fri . "Structure of the GH1 domain of guanylate kinase-associated protein from Rattus norvegicus". United States. doi:10.1016/J.BBRC.2014.08.073.
@article{osti_22416741,
title = {Structure of the GH1 domain of guanylate kinase-associated protein from Rattus norvegicus},
author = {Tong, Junsen and Yang, Huiseon and Eom, Soo Hyun and Chun, ChangJu, E-mail: cchun1130@jnu.ac.kr and Im, Young Jun, E-mail: imyoungjun@jnu.ac.kr},
abstractNote = {Graphical abstract: - Highlights: • The crystal structure of GKAP homology domain 1 (GH1) was determined. • GKAP GH1 is a three-helix bundle connected by short flexible loops. • The predicted helix α4 associates weakly with the helix α3, suggesting dynamic nature of the GH1 domain. - Abstract: 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 Å resolution. The structure of GKAP GH1 displays a three-helix bundle connected by short flexible loops. The predicted helix α4 which was not visible in the crystal structure associates weakly with the helix α3 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.},
doi = {10.1016/J.BBRC.2014.08.073},
journal = {Biochemical and Biophysical Research Communications},
issn = {0006-291X},
number = 1,
volume = 452,
place = {United States},
year = {2014},
month = {9}
}