1gc1: Difference between revisions
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[[Image:1gc1.gif|left|200px]] | [[Image:1gc1.gif|left|200px]] | ||
'''HIV-1 GP120 CORE COMPLEXED WITH CD4 AND A NEUTRALIZING HUMAN ANTIBODY''' | {{Structure | ||
|PDB= 1gc1 |SIZE=350|CAPTION= <scene name='initialview01'>1gc1</scene>, resolution 2.5Å | |||
|SITE= <scene name='pdbsite=O:Water+Hoh+1000+(Zero+Occupancy)+Marks+The+Location+Of+Ce+...'>O</scene> | |||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''HIV-1 GP120 CORE COMPLEXED WITH CD4 AND A NEUTRALIZING HUMAN ANTIBODY''' | |||
==Overview== | ==Overview== | ||
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. | 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. | ||
==About this Structure== | ==About this Structure== | ||
1GC1 is a [ | 1GC1 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GC1 OCA]. | ||
==Reference== | ==Reference== | ||
Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody., Kwong PD, Wyatt R, Robinson J, Sweet RW, Sodroski J, Hendrickson WA, Nature. 1998 Jun 18;393(6686):648-59. PMID:[http:// | Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody., Kwong PD, Wyatt R, Robinson J, Sweet RW, Sodroski J, Hendrickson WA, Nature. 1998 Jun 18;393(6686):648-59. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9641677 9641677] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Human immunodeficiency virus 1]] | [[Category: Human immunodeficiency virus 1]] | ||
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[[Category: t-cell surface glycoprotein cd4]] | [[Category: t-cell surface glycoprotein cd4]] | ||
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