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1czq

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(New page: 200px<br /> <applet load="1czq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1czq, resolution 1.50&Aring;" /> '''CRYSTAL STRUCTURE O...)
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[[Image:1czq.gif|left|200px]]<br /><applet load="1czq" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1czq" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1czq, resolution 1.50&Aring;" />
caption="1czq, resolution 1.50&Aring;" />
'''CRYSTAL STRUCTURE OF THE D10-P1/IQN17 COMPLEX: A D-PEPTIDE INHIBITOR OF HIV-1 ENTRY BOUND TO THE GP41 COILED-COIL POCKET.'''<br />
'''CRYSTAL STRUCTURE OF THE D10-P1/IQN17 COMPLEX: A D-PEPTIDE INHIBITOR OF HIV-1 ENTRY BOUND TO THE GP41 COILED-COIL POCKET.'''<br />
==Overview==
==Overview==
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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.
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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 Structure==
==About this Structure==
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1CZQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_and_human_immunodeficiency_virus Saccharomyces cerevisiae and human immunodeficiency virus] with CL and ACE as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CZQ OCA].
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1CZQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_and_human_immunodeficiency_virus Saccharomyces cerevisiae and human immunodeficiency virus] with <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CZQ OCA].
==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae and human immunodeficiency virus]]
[[Category: Saccharomyces cerevisiae and human immunodeficiency virus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Carr, P.A.]]
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[[Category: Carr, P A.]]
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[[Category: Eckert, D.M.]]
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[[Category: Eckert, D M.]]
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[[Category: Hong, L.H.]]
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[[Category: Hong, L H.]]
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[[Category: Kim, P.S.]]
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[[Category: Kim, P S.]]
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[[Category: Malashkevich, V.N.]]
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[[Category: Malashkevich, V N.]]
[[Category: ACE]]
[[Category: ACE]]
[[Category: CL]]
[[Category: CL]]
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[[Category: envelope glycoprotein]]
[[Category: envelope glycoprotein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov 8 13:57:26 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:11:21 2008''

Revision as of 10:11, 21 February 2008


1czq, resolution 1.50Å

Drag the structure with the mouse to rotate

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

Overview

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 Structure

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

Reference

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

Page seeded by OCA on Thu Feb 21 12:11:21 2008

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