کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
442981 692450 2007 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Molecular dynamics analysis of HIV-1 matrix protein: Clarifying differences between crystallographic and solution structures
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی تئوریک و عملی
پیش نمایش صفحه اول مقاله
Molecular dynamics analysis of HIV-1 matrix protein: Clarifying differences between crystallographic and solution structures
چکیده انگلیسی

One of the main structural features of the mature HIV-1 virion is the matrix protein (p17). This partially globular protein presents four helixes centrally organized and a fifth one, H5, projecting away from the packed bundle of helixes. Comparison between solution and crystallographic data of p17 indicates a 6 Å displacement of a short 310 helix and a partial unfolding of H5 in solution related to crystal. While the behavior of the 310 helix has been previously addressed to virion assembly, the relevance and origin of H5 partial unfolding is possibly related to the contacts between p17 and other viral elements, such as p24. In this context, we present a 40 ns conformational sampling of monomeric p17 using molecular dynamics simulations. The performed simulations presented a progressive conversion of the p17 crystallographic structure to the NMR conformation, suggesting that the biological form of this protein may have its C-terminal portion partially unfolded.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Molecular Graphics and Modelling - Volume 26, Issue 1, July 2007, Pages 62–68
نویسندگان
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