1HIW

TRIMERIC HIV-1 MATRIX PROTEIN

Summary for 1HIW

• Entry DOI: 10.2210/pdb1hiw/pdb
• Descriptor: HIV-1 MATRIX PROTEIN, SULFATE ION (3 entities in total)
• Functional Keywords: hiv-1, p17, hiv-1 ma, matrix protein
• Biological source: Human immunodeficiency virus 1
• Cellular location: Matrix protein p17: Virion (Potential). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential): P12493
• Total number of polymer chains: 6
• Total formula weight: 90792.25

Authors

Hill, C.P.,Worthylake, D.,Bancroft, D.P.,Christensen, A.M.,Sundquist, W.I. (deposition date: 1996-02-28, release date: 1996-10-14, Last modification date: 2024-02-07)

Primary citation

Hill, C.P.,Worthylake, D.,Bancroft, D.P.,Christensen, A.M.,Sundquist, W.I.
Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: implications for membrane association and assembly.
Proc.Natl.Acad.Sci.USA, 93:3099-3104, 1996

PubMed Abstract: 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.

PubMed: 8610175
DOI: 10.1073/pnas.93.7.3099

Experimental method

X-RAY DIFFRACTION (2.3 Å)