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Title: Targeted molecular dynamics simulation studies of calcium binding and conformational change in the C-terminal half of gelsolin

Abstract

Gelsolin consists of six related domains (G1-G6) and the C-terminal half (G4-G6) acts as a calcium sensor during the activation of the whole molecule, a process that involves large domain movements. In this study, we used targeted molecular dynamics simulations to elucidate the conformational transitions of G4-G6 at an atomic level. Domains G4 and G6 are initially ruptured, followed by a rotation of G6 by {approx}90{sup o}, which is the dominant conformational change. During this period, local conformational changes occur at the G4 and G5 calcium-binding sites, facilitating large changes in interdomain distances. Alterations in the binding affinities of the calcium ions in these three domains appear to be related to local conformational changes at their binding sites. Analysis of the relative stabilities of the G4-G6-bound calcium ions suggests that they bind first to G6, then to G4, and finally to G5.

Authors:
 [1];  [2];  [3];  [1];  [2];  [1];  [2];  [4];  [5]
  1. Department of Microbiology, University of Ulsan College of Medicine, 388-1 PoongNap-dong Songpa-goo, Seoul 138-736 (Korea, Republic of)
  2. (Korea, Republic of)
  3. Institute of Molecular and Cell Biology, Proteos, 61 Biopolis Drive, 138673 Singapore (Singapore)
  4. Department of Microbiology, University of Ulsan College of Medicine, 388-1 PoongNap-dong Songpa-goo, Seoul 138-736 (Korea, Republic of) and Research Institute for Biomacromolecules, University of Ulsan College of Medicine, 388-1 PoongNap-dong Songpa-goo, Seoul 138-736 (Korea, Republic of). E-mail: ykkim@amc.seoul.kr
  5. Department of Physiology, University of Ulsan College of Medicine, 388-1 PoongNap-dong Songpa-goo, Seoul 138-736 (Korea, Republic of) and Research Institute for Biomacromolecules, University of Ulsan College of Medicine, 388-1 PoongNap-dong Songpa-goo, Seoul 138-736 (Korea, Republic of). E-mail: hchoe@amc.seoul.kr
Publication Date:
OSTI Identifier:
20798887
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 342; Journal Issue: 3; Other Information: DOI: 10.1016/j.bbrc.2006.01.184; PII: S0006-291X(06)00204-X; Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; CALCIUM; CALCIUM IONS; CONFORMATIONAL CHANGES; MOLECULAR DYNAMICS METHOD; MOLECULES; SIMULATION

Citation Formats

Lee, Hui Sun, Research Institute for Biomacromolecules, University of Ulsan College of Medicine, 388-1 PoongNap-dong Songpa-goo, Seoul 138-736, Robinson, Robert Charles, Joo, Chul Hyun, Research Institute for Biomacromolecules, University of Ulsan College of Medicine, 388-1 PoongNap-dong Songpa-goo, Seoul 138-736, Lee, Heuiran, Research Institute for Biomacromolecules, University of Ulsan College of Medicine, 388-1 PoongNap-dong Songpa-goo, Seoul 138-736, Kim, Yoo Kyum, and Choe, Han. Targeted molecular dynamics simulation studies of calcium binding and conformational change in the C-terminal half of gelsolin. United States: N. p., 2006. Web. doi:10.1016/j.bbrc.2006.01.184.
Lee, Hui Sun, Research Institute for Biomacromolecules, University of Ulsan College of Medicine, 388-1 PoongNap-dong Songpa-goo, Seoul 138-736, Robinson, Robert Charles, Joo, Chul Hyun, Research Institute for Biomacromolecules, University of Ulsan College of Medicine, 388-1 PoongNap-dong Songpa-goo, Seoul 138-736, Lee, Heuiran, Research Institute for Biomacromolecules, University of Ulsan College of Medicine, 388-1 PoongNap-dong Songpa-goo, Seoul 138-736, Kim, Yoo Kyum, & Choe, Han. Targeted molecular dynamics simulation studies of calcium binding and conformational change in the C-terminal half of gelsolin. United States. doi:10.1016/j.bbrc.2006.01.184.
Lee, Hui Sun, Research Institute for Biomacromolecules, University of Ulsan College of Medicine, 388-1 PoongNap-dong Songpa-goo, Seoul 138-736, Robinson, Robert Charles, Joo, Chul Hyun, Research Institute for Biomacromolecules, University of Ulsan College of Medicine, 388-1 PoongNap-dong Songpa-goo, Seoul 138-736, Lee, Heuiran, Research Institute for Biomacromolecules, University of Ulsan College of Medicine, 388-1 PoongNap-dong Songpa-goo, Seoul 138-736, Kim, Yoo Kyum, and Choe, Han. Fri . "Targeted molecular dynamics simulation studies of calcium binding and conformational change in the C-terminal half of gelsolin". United States. doi:10.1016/j.bbrc.2006.01.184.
@article{osti_20798887,
title = {Targeted molecular dynamics simulation studies of calcium binding and conformational change in the C-terminal half of gelsolin},
author = {Lee, Hui Sun and Research Institute for Biomacromolecules, University of Ulsan College of Medicine, 388-1 PoongNap-dong Songpa-goo, Seoul 138-736 and Robinson, Robert Charles and Joo, Chul Hyun and Research Institute for Biomacromolecules, University of Ulsan College of Medicine, 388-1 PoongNap-dong Songpa-goo, Seoul 138-736 and Lee, Heuiran and Research Institute for Biomacromolecules, University of Ulsan College of Medicine, 388-1 PoongNap-dong Songpa-goo, Seoul 138-736 and Kim, Yoo Kyum and Choe, Han},
abstractNote = {Gelsolin consists of six related domains (G1-G6) and the C-terminal half (G4-G6) acts as a calcium sensor during the activation of the whole molecule, a process that involves large domain movements. In this study, we used targeted molecular dynamics simulations to elucidate the conformational transitions of G4-G6 at an atomic level. Domains G4 and G6 are initially ruptured, followed by a rotation of G6 by {approx}90{sup o}, which is the dominant conformational change. During this period, local conformational changes occur at the G4 and G5 calcium-binding sites, facilitating large changes in interdomain distances. Alterations in the binding affinities of the calcium ions in these three domains appear to be related to local conformational changes at their binding sites. Analysis of the relative stabilities of the G4-G6-bound calcium ions suggests that they bind first to G6, then to G4, and finally to G5.},
doi = {10.1016/j.bbrc.2006.01.184},
journal = {Biochemical and Biophysical Research Communications},
number = 3,
volume = 342,
place = {United States},
year = {Fri Apr 14 00:00:00 EDT 2006},
month = {Fri Apr 14 00:00:00 EDT 2006}
}