1hiw
From Proteopedia
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TRIMERIC HIV-1 MATRIX PROTEIN
Overview
The human immunodeficiency virus type 1 (HIV-1) matrix protein forms a, structural shell associated with the inner viral membrane and performs, other essential functions throughout the viral life cycle. The crystal, structure of the HIV-1 matrix protein, determined at 2.3 angstrom, resolution, reveals that individual matrix molecules are composed of five, major helices capped by a three-stranded mixed beta-sheet. Unexpectedly, the protein assembles into a trimer in three different crystal lattices, burying 1880 angstrom2 of accessible surface area at the trimer, interfaces. Trimerization appears to create a large, bipartite membrane, binding surface in which exposed basic residues could cooperate with the, N-terminal myristoyl groups to anchor the protein on the acidic inner, membrane of the virus.
About this Structure
1HIW is a Single protein structure of sequence from Human immunodeficiency virus with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: implications for membrane association and assembly., Hill CP, Worthylake D, Bancroft DP, Christensen AM, Sundquist WI, Proc Natl Acad Sci U S A. 1996 Apr 2;93(7):3099-104. PMID:8610175
Page seeded by OCA on Thu Nov 8 14:06:05 2007
