Article ID Journal Published Year Pages File Type
442981 Journal of Molecular Graphics and Modelling 2007 7 Pages PDF
Abstract

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.

Related Topics
Physical Sciences and Engineering Chemistry Physical and Theoretical Chemistry
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