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• W2090231185 startingPage "1104" @default.
• W2090231185 abstract "Abstract Protein flexibility and conformational diversity is well known to be a key characteristic of the function of many proteins. Human blood coagulation proteins have multiple substrates, and various protein–protein interactions are required for the smooth functioning of the coagulation cascade to maintain blood hemostasis. To address how a protein may cope with multiple interactions with its structurally diverse substrates and the accompanied structural changes that may drive these changes, we studied human Factor X. We employed 20 ns of molecular dynamics (MD) and steered molecular dynamics (SMD) simulations on two different conformational forms of Factor X, open and closed, and observed an interchangeable conformational transition from one to another. This work also demonstrates the roles of various aromatic residues involved in aromatic–aromatic interactions, which make this dynamic transition possible. © 2008 Wiley Periodicals, Inc. Biopolymers 89: 1104–1113, 2008. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com" @default.
• W2090231185 created "2016-06-24" @default.
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• W2090231185 date "2008-08-04" @default.
• W2090231185 modified "2023-10-17" @default.
• W2090231185 title "Molecular dynamics simulations of Factor Xa: Insight into conformational transition of its binding subsites" @default.
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• W2090231185 doi "https://doi.org/10.1002/bip.21062" @default.
• W2090231185 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5030816" @default.
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