1qr9

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<StructureSection load='1qr9' size='340' side='right'caption='[[1qr9]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='1qr9' size='340' side='right'caption='[[1qr9]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1qr9]] is a 1 chain structure with sequence from [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=1QR9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QR9 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1qr9]] is a 1 chain structure with sequence from [https://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=1QR9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QR9 FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qr9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qr9 OCA], [http://pdbe.org/1qr9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qr9 RCSB], [http://www.ebi.ac.uk/pdbsum/1qr9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qr9 ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qr9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qr9 OCA], [https://pdbe.org/1qr9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qr9 RCSB], [https://www.ebi.ac.uk/pdbsum/1qr9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qr9 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q76270_9HIV1 Q76270_9HIV1]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qr9 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qr9 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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The gp41 envelope protein of human immunodeficiency virus type 1 (HIV-1) contains an alpha-helical core structure responsible for mediating membrane fusion during viral entry. Recent studies suggest that a conserved hydrophobic cavity in the coiled coil of this core plays a distinctive structural role in maintaining the fusogenic conformation of the gp41 molecule. Here we investigated the importance of this cavity in determining the structure and biological activity of the gp41 core by using the N34(L6)C28 model. The high-resolution crystal structures of N34(L6)C28 of two HIV-1 gp41 fusion-defective mutants reveal that each mutant sequence is accommodated in the six-helix bundle structure by forming the cavity with different sets of atoms. Remarkably, the mutant N34(L6)C28 cores are highly effective inhibitors of HIV-1 infection, with 5- to 16-fold greater activity than the wild-type molecule. The enhanced inhibitory activity by fusion-defective mutations correlates with local structural perturbations close to the cavity that destabilize the six-helix bundle. Taken together, these results indicate that the conserved hydrophobic coiled-coil cavity in the gp41 core is critical for HIV-1 entry and its inhibition and provides a potential antiviral drug target.
 
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Inhibition of human immunodeficiency virus type 1 infectivity by the gp41 core: role of a conserved hydrophobic cavity in membrane fusion.,Ji H, Shu W, Burling FT, Jiang S, Lu M J Virol. 1999 Oct;73(10):8578-86. PMID:10482611<ref>PMID:10482611</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1qr9" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Gp41 3D Structures|Gp41 3D Structures]]
*[[Gp41 3D Structures|Gp41 3D Structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human immunodeficiency virus 1]]
[[Category: Human immunodeficiency virus 1]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Burling, F T]]
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[[Category: Burling FT]]
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[[Category: Ji, H]]
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[[Category: Ji H]]
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[[Category: Jiang, S B]]
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[[Category: Jiang SB]]
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[[Category: Lu, M]]
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[[Category: Lu M]]
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[[Category: Shu, W]]
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[[Category: Shu W]]
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[[Category: Gp41]]
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[[Category: Hiv-1 envelope protein]]
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[[Category: Hiv-1 inhibition]]
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[[Category: Membrane fusion]]
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[[Category: Viral protein]]
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Current revision

INHIBITION OF HIV-1 INFECTIVITY BY THE GP41 CORE: ROLE OF A CONSERVED HYDROPHOBIC CAVITY IN MEMBRANE FUSION

PDB ID 1qr9

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