1hek | pdb_00001hek

Crystal structure of equine infectious anaemia virus matrix antigen (EIAV MA)

spinqualitylabelsall models 1hek, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1hek is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: MSE Related: 1eia, 2eia Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Gag polyprotein

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