1hek

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Revision as of 17:25, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1hek" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hek, resolution 2.80Å" /> '''CRYSTAL STRUCTURE OF...)
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File:1hek.gif


1hek, resolution 2.80Å

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CRYSTAL STRUCTURE OF EQUINE INFECTIOUS ANAEMIA VIRUS MATRIX ANTIGEN (EIAV MA)

OverviewOverview

The Gag polyprotein is key to the budding of retroviruses from host cells, and is cleaved upon virion maturation, the N-terminal membrane-binding, domain forming the matrix protein (MA). The 2.8-A resolution crystal, structure of MA of equine infectious anemia virus (EIAV), a lentivirus, reveals that, despite showing no sequence similarity, more than half of, the molecule can be superimposed on the MAs of human immunodeficiency, virus type 1 (HIV-1) and simian immunodeficiency virus (SIV). However, unlike the structures formed by HIV-1 and SIV MAs, the oligomerization, state observed is not trimeric. We discuss the potential of this molecule, for membrane binding in the light of conformational differences between, EIAV MA and HIV or SIV MA.

About this StructureAbout this Structure

1HEK is a Single protein structure of sequence from Equine infectious anemia virus. Full crystallographic information is available from OCA.

ReferenceReference

Structure of equine infectious anemia virus matrix protein., Hatanaka H, Iourin O, Rao Z, Fry E, Kingsman A, Stuart DI, J Virol. 2002 Feb;76(4):1876-83. PMID:11799182

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