This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1hiw
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1hiw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hiw, resolution 2.3Å" /> '''TRIMERIC HIV-1 MATRI...)
Next diff →
Revision as of 12:00, 8 November 2007
|
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
