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 ∼90°, 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.
| Original language | English |
|---|---|
| Pages (from-to) | 702-709 |
| Number of pages | 8 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 342 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Apr 14 2006 |
| Externally published | Yes |
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Keywords
- Calcium binding
- Conformational change
- Gelsolin C-terminal half
- Targeted molecular dynamics simulation
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology
Cite this
Targeted molecular dynamics simulation studies of calcium binding and conformational change in the C-terminal half of gelsolin. / Lee, Hui Sun; Robinson, Robert Charles; Joo, Chul Hyun; Lee, Heuiran; Kim, Yoo Kyum; Choe, Han.
In: Biochemical and Biophysical Research Communications, Vol. 342, No. 3, 14.04.2006, p. 702-709.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Targeted molecular dynamics simulation studies of calcium binding and conformational change in the C-terminal half of gelsolin
AU - Lee, Hui Sun
AU - Robinson, Robert Charles
AU - Joo, Chul Hyun
AU - Lee, Heuiran
AU - Kim, Yoo Kyum
AU - Choe, Han
PY - 2006/4/14
Y1 - 2006/4/14
N2 - 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 ∼90°, 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.
AB - 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 ∼90°, 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.
KW - Calcium binding
KW - Conformational change
KW - Gelsolin C-terminal half
KW - Targeted molecular dynamics simulation
UR - http://www.scopus.com/inward/record.url?scp=33644619833&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=33644619833&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2006.01.184
DO - 10.1016/j.bbrc.2006.01.184
M3 - Article
C2 - 16494841
AN - SCOPUS:33644619833
VL - 342
SP - 702
EP - 709
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -