2bf1
From Proteopedia
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STRUCTURE OF AN UNLIGANDED AND FULLY-GLYCOSYLATED SIV GP120 ENVELOPE GLYCOPROTEIN
Overview
Envelope glycoproteins of human and simian immunodeficiency virus (HIV and, SIV) undergo a series of conformational changes when they interact with, receptor (CD4) and co-receptor on the surface of a potential host cell, leading ultimately to fusion of viral and cellular membranes. Structures, of fragments of gp120 and gp41 from the envelope protein are known, in, conformations corresponding to their post-attachment and postfusion, states, respectively. We report the crystal structure, at 4 A resolution, of a fully glycosylated SIV gp120 core, in a conformation representing its, prefusion state, before interaction with CD4. Parts of the protein have a, markedly different organization than they do in the CD4-bound state., Comparison of the unliganded and CD4-bound structures leads to a model for, events that accompany receptor engagement of an envelope glycoprotein, trimer. The two conformations of gp120 also present distinct antigenic, surfaces. We identify the binding site for a compound that inhibits viral, entry.
About this Structure
2BF1 is a Single protein structure of sequence from Simian immunodeficiency virus with NAG and MAN as ligands. Full crystallographic information is available from OCA.
Reference
Structure of an unliganded simian immunodeficiency virus gp120 core., Chen B, Vogan EM, Gong H, Skehel JJ, Wiley DC, Harrison SC, Nature. 2005 Feb 24;433(7028):834-41. PMID:15729334
Page seeded by OCA on Wed Nov 21 08:46:09 2007
Categories: Simian immunodeficiency virus | Single protein | Chen, B. | Gong, H. | Harrison, S.C. | Skehel, J.J. | Vogan, E.M. | Wiley, D.C. | MAN | NAG | Aids | Coat protein | Envelope glycoprotein | Gp120 | Siv
