1a43
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STRUCTURE OF THE HIV-1 CAPSID PROTEIN DIMERIZATION DOMAIN AT 2.6A RESOLUTION
OverviewOverview
The human immunodeficiency virus type I (HIV-1) capsid protein is, initially synthesized as the central domain of the Gag polyprotein, and is, subsequently proteolytically processed into a discrete 231-amino-acid, protein that forms the distinctive conical core of the mature virus. The, crystal structures of two proteins that span the C-terminal domain of the, capsid are reported here: one encompassing residues 146-231 (CA146-231), and the other extending to include the 14-residue p2 domain of Gag, (CA146-p2). The isomorphous CA146-231 and CA146-p2 structures were, determined by molecular replacement and have been refined at 2.6 A, resolution to R factors of 22.3 and 20.7% (Rfree = 28.1 and 27.5%), respectively. The ordered domains comprise residues 148-219 for CA146-231, and 148-218 for CA146-p2, and their refined structures are essentially, identical. The proteins are composed of a 310 helix followed by an, extended strand and four alpha-helices. A crystallographic twofold, generates a dimer that is stabilized by parallel packing of an alpha-helix, 2 across the dimer interface and by packing of the 310 helix into a groove, created by alpha-helices 2 and 3 of the partner molecule. CA146-231 and, CA146-p2 dimerize with the full affinity of the intact capsid protein, and, their structures therefore reveal the essential dimer interface of the, HIV-1 capsid.
About this StructureAbout this Structure
1A43 is a Single protein structure of sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.
ReferenceReference
Structures of the HIV-1 capsid protein dimerization domain at 2.6 A resolution., Worthylake DK, Wang H, Yoo S, Sundquist WI, Hill CP, Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):85-92. Epub 1999, Jan 1. PMID:10089398
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