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.
1gc1
From Proteopedia
| Line 5: | Line 5: | ||
==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 .. | + | 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 [http://en.wikipedia.org/wiki/Protein_complex 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] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: O. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GC1 OCA]. |
==Reference== | ==Reference== | ||
| Line 28: | Line 28: | ||
[[Category: t-cell surface glycoprotein cd4]] | [[Category: t-cell surface glycoprotein cd4]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:26:16 2007'' |
Revision as of 13:20, 5 November 2007
|
HIV-1 GP120 CORE COMPLEXED WITH CD4 AND A NEUTRALIZING HUMAN ANTIBODY
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.
About this Structure
1GC1 is a Protein complex structure of sequences from Homo sapiens and Human immunodeficiency virus 1 with NAG as ligand. Structure known Active Site: O. Full crystallographic information is available from OCA.
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:9641677
Page seeded by OCA on Mon Nov 5 15:26:16 2007
Categories: Homo sapiens | Human immunodeficiency virus 1 | Protein complex | Hendrickson, W.A. | Kwong, P.D. | Robinson, J. | Sodroski, J. | Sweet, R.W. | Wyatt, R. | NAG | Antigen-binding fragment of human immunoglobulin 17b | Complex (hiv envelope protein/cd4/fab) | Glycosylated protein | Hiv-1 exterior envelope gp120 | T-cell surface glycoprotein cd4
