Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: implications for membrane association and assembly.
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.
Hill
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CP
Department of Biochemistry, University of Utah, Salt Lake City, 84132, USA.
Worthylake
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D
Bancroft
D P
DP
Christensen
A M
AM
Sundquist
W I
WI
D003198:Computer Simulation; D018360:Crystallography, X-Ray; D015497:HIV-1 / Q000378:metabolism* / Q000502:physiology; D006801:Humans; D046911:Macromolecular Substances; D008561:Membrane Fusion; D008563:Membrane Lipids; D008958:Models, Molecular; D010743:Phospholipids; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000378:metabolism; D014763:Viral Matrix Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000378:metabolism*
D046911:Macromolecular Substances; D008563:Membrane Lipids; D010743:Phospholipids; D011994:Recombinant Proteins; D014763:Viral Matrix Proteins