1czq

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Revision as of 14:51, 8 November 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="1czq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1czq, resolution 1.50Å" /> '''CRYSTAL STRUCTURE O...)
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File:1czq.gif


1czq, resolution 1.50Å

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CRYSTAL STRUCTURE OF THE D10-P1/IQN17 COMPLEX: A D-PEPTIDE INHIBITOR OF HIV-1 ENTRY BOUND TO THE GP41 COILED-COIL POCKET.

OverviewOverview

The HIV-1 gp41 protein promotes viral entry by mediating the fusion of, viral and cellular membranes. A prominent pocket on the surface of a, central trimeric coiled coil within gp41 was previously identified as a, potential target for drugs that inhibit HIV-1 entry. We designed a, peptide, IQN17, which properly presents this pocket. Utilizing IQN17 and, mirror-image phage display, we identified cyclic, D-peptide inhibitors of, HIV-1 infection that share a sequence motif. A 1.5 A cocrystal structure, of IQN17 in complex with a D-peptide, and NMR studies, show that conserved, residues of these inhibitors make intimate contact with the gp41 pocket., Our studies validate the pocket per se as a target for drug development., IQN17 and these D-peptide inhibitors are likely to be useful for, development and identification of a new class of orally bioavailable, anti-HIV drugs.

About this StructureAbout this Structure

1CZQ is a Single protein structure of sequence from Saccharomyces cerevisiae and human immunodeficiency virus with CL and ACE as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Inhibiting HIV-1 entry: discovery of D-peptide inhibitors that target the gp41 coiled-coil pocket., Eckert DM, Malashkevich VN, Hong LH, Carr PA, Kim PS, Cell. 1999 Oct 1;99(1):103-15. PMID:10520998

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