Abstract:
:The solution structures of the N-terminal domains of protein S, a plasma vitamin K-dependent glycoprotein, and its homolog growth arrest specific protein 6 (Gas6) were predicted by molecular dynamics computer simulations. The initial structures were based on the x-ray crystallographic structure of the corresponding region of bovine prothrombin fragment 1. The subsequent molecular dynamics trajectories were calculated using the second-generation AMBER force field. The long-range electrostatic forces were evaluated by the particle mesh Ewald method. The structures that stabilized over a 400-ps time interval were compared with the corresponding region of the simulated solution structure of bovine prothrombin fragment 1. Structural properties of the gamma-carboxyglutamic acid (Gla) domains obtained from simulations and calcium binding were found to be conserved for all three proteins. Analysis of the predicted solution structure of the Gla domain of Gas6 suggests that this domain should bind with negatively charged phospholipid surfaces analogous to bovine prothrombin fragment 1 and protein S.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Perera L,Li L,Darden T,Monroe DM,Pedersen LGdoi
10.1016/S0006-3495(97)78215-8subject
Has Abstractpub_date
1997-10-01 00:00:00pages
1847-56issue
4eissn
0006-3495issn
1542-0086pii
S0006-3495(97)78215-8journal_volume
73pub_type
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