Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: implications for membrane association and assembly. NLM AIDSLINE Important note: Information in this article was accurate in 1996. The state of the art may have changed since the publication date.

Click here to return to AIDSLINE main menu
DonateNow
Print this Article


Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: implications for membrane association and assembly.

Proc Natl Acad Sci U S A. 1996 Apr 2;93(7):3099-104. Unique Identifier : AIDSLINE MED/96181540
Hill CP; Worthylake D; Bancroft DP; Christensen AM; Sundquist WI; Department of Biochemistry, University of Utah, Salt Lake City,; 84132, USA.

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.
Keywords: Computer Simulation Crystallography, X-Ray Human HIV-1/*METABOLISM/PHYSIOLOGY Macromolecular Systems *Membrane Fusion Membrane Lipids Models, Molecular Phospholipids *Protein Structure, Secondary Recombinant Proteins/BIOSYNTHESIS/CHEMISTRY/METABOLISM Support, Non-U.S. Gov't Support, U.S. Gov't, P.H.S. Viral Matrix Proteins/BIOSYNTHESIS/*CHEMISTRY/*METABOLISM JOURNAL ARTICLEKWDcomputersimulationcrystallography,x-rayhumanhiv-1/KWDmetabolism/physiologymacromolecularsystemsKWDmembranefusionmembranelipidsmodels,molecularphospholipidsKWDproteinstructure,secondaryrecombinantproteins/biosynthesis/chemistry/metabolismsupport,non-uKWDsKWDgov'tsupport,uKWDsKWDgov't,pKWDhKWDsKWDviralmatrixproteins/biosynthesis/KWDchemistry/KWDmetabolismjournalarticle
960830
M9681145

Copyright © 1996 - National Library of Medicine. Reproduced under license with the National Library of Medicine, Bethesda, MD.

AEGiS is a 501(c)3, not-for-profit, tax-exempt, educational corporation. AEGiS is made possible through unrestricted funding from Boehringer Ingelheim, Bridgestone/Firestone Charitable Trust, Bristol-Myers Squibb Company, Elton John AIDS Foundation, Gill Foundation, the National Library of Medicine, Quest Diagnostics, Roche and Trimeris, and donations from users like you. Always watch for outdated information. This article first appeared in 1996. This material is designed to support, not replace, the relationship that exists between you and your doctor.

AEGiS presents published material, reprinted with permission and neither endorses nor opposes any material. All information contained on this website, including information relating to health conditions, products, and treatments, is for informational purposes only. It is often presented in summary or aggregate form. It is not meant to be a substitute for the advice provided by your own physician or other medical professionals. Always discuss treatment options with a doctor who specializes in treating HIV.

Copyright ©1980, 1996. AEGiS. All materials appearing on AEGiS are protected by copyright as a collective work or compilation under U.S. copyright and other laws and are the property of AEGiS, or the party credited as the provider of the content. .