1nj0
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(New page: 200px<br /> <applet load="1nj0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nj0" /> '''NMR structure of a V3 (MN isolate) peptide ...)
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Revision as of 12:15, 8 November 2007
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NMR structure of a V3 (MN isolate) peptide bound to 447-52D, a human HIV-1 neutralizing antibody
Overview
The V3 loop of the HIV-1 envelope glycoprotein gp120 is involved in, binding to the CCR5 and CXCR4 coreceptors. The structure of an HIV-1(MN), V3 peptide bound to the Fv of the broadly neutralizing human monoclonal, antibody 447-52D was solved by NMR and found to be a beta hairpin. This, structure of V3(MN) was found to have conformation and sequence, similarities to beta hairpins in CD8 and CCR5 ligands MIP-1alpha, MIP-1beta, and RANTES and differed from the beta hairpin of a V3(IIIB), peptide bound to the strain-specific murine anti-gp120(IIIB) antibody, 0.5beta. In contrast to the structure of the bound V3(MN) peptide, the, V3(IIIB) peptide resembles a beta hairpin in SDF-1, a CXCR4 ligand. These, data suggest that the 447-52D-bound V3(MN) and the 0.5beta-bound V3(IIIB), structures represent alternative V3 conformations responsible for, selective interactions with CCR5 and CXCR4, respectively.
About this Structure
1NJ0 is a Single protein structure of sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.
Reference
Alternative conformations of HIV-1 V3 loops mimic beta hairpins in chemokines, suggesting a mechanism for coreceptor selectivity., Sharon M, Kessler N, Levy R, Zolla-Pazner S, Gorlach M, Anglister J, Structure. 2003 Feb;11(2):225-36. PMID:12575942
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