1GC1: Hiv-1 Gp120 Core Complexed With CD4 and a Neutralizing Human Antibody

Citation:
Abstract
The entry of human immunodeficiency virus (HIV) into cells requires the sequential interaction of the viral exterior envelope glycoprotein, gp120, with the CD4 glycoprotein and a chemokine receptor on the cell surface. These interactions initiate a fusion of the viral and cellular membranes. Although gp120 can elicit virus-neutralizing antibodies, HIV eludes the immune system. We have solved the X-ray crystal structure at 2.5 A resolution of an HIV-1 gp120 core complexed with a two-domain fragment of human CD4 and an antigen-binding fragment of a neutralizing antibody that blocks chemokine-receptor binding. The structure reveals a cavity-laden CD4-gp120 interface, a conserved binding site for the chemokine receptor, evidence for a conformational change upon CD4 binding, the nature of a CD4-induced antibody epitope, and specific mechanisms for immune evasion. Our results provide a framework for understanding the complex biology of HIV entry into cells and should guide efforts to intervene.
PDB ID: 1GC1Download
MMDB ID: 8099
PDB Deposition Date: 1998/6/15
Updated in MMDB: 1998/11 
Experimental Method:
x-ray diffraction
Resolution: 2.5  Å
Source Organism:
Human immunodeficiency virus 1
Similar Structures:
Biological Unit for 1GC1: tetrameric; determined by author
Molecular Components in 1GC1
Label Count Molecule
Proteins (4 molecules)
1
Envelope Protein Gp120
Molecule annotation
1
CD4
Molecule annotation
1
Antibody 17B
Molecule annotation
1
Antibody 17B
Molecule annotation
Chemicals (15 molecules)
1
10
2
1
3
4
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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