4b4n: Difference between revisions
New page: '''Unreleased structure''' The entry 4b4n is ON HOLD Authors: Price, A.J., James, L.C. Description: CPSF6 defines a conserved capsid interface that modulates HIV-1 replication |
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The entry | ==CPSF6 defines a conserved capsid interface that modulates HIV-1 replication== | ||
<StructureSection load='4b4n' size='340' side='right'caption='[[4b4n]], [[Resolution|resolution]] 1.81Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4b4n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [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=4B4N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B4N FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.813Å</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4b4n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b4n OCA], [https://pdbe.org/4b4n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b4n RCSB], [https://www.ebi.ac.uk/pdbsum/4b4n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b4n ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A9PKC6_9HIV1 A9PKC6_9HIV1] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The HIV-1 genome enters cells inside a shell comprised of capsid (CA) protein. Variation in CA sequence alters HIV-1 infectivity and escape from host restriction factors. However, apart from the Cyclophilin A-binding loop, CA has no known interfaces with which to interact with cellular cofactors. Here we describe a novel protein-protein interface in the N-terminal domain of HIV-1 CA, determined by X-ray crystallography, which mediates both viral restriction and host cofactor dependence. The interface is highly conserved across lentiviruses and is accessible in the context of a hexameric lattice. Mutation of the interface prevents binding to and restriction by CPSF6-358, a truncated cytosolic form of the RNA processing factor, cleavage and polyadenylation specific factor 6 (CPSF6). Furthermore, mutations that prevent CPSF6 binding also relieve dependence on nuclear entry cofactors TNPO3 and RanBP2. These results suggest that the HIV-1 capsid mediates direct host cofactor interactions to facilitate viral infection. | |||
CPSF6 Defines a Conserved Capsid Interface that Modulates HIV-1 Replication.,Price AJ, Fletcher AJ, Schaller T, Elliott T, Lee K, Kewalramani VN, Chin JW, Towers GJ, James LC PLoS Pathog. 2012 Aug;8(8):e1002896. Epub 2012 Aug 30. PMID:22956906<ref>PMID:22956906</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4b4n" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Human immunodeficiency virus 1]] | |||
[[Category: Large Structures]] | |||
[[Category: James LC]] | |||
[[Category: Price AJ]] | |||
Latest revision as of 14:43, 20 December 2023
CPSF6 defines a conserved capsid interface that modulates HIV-1 replicationCPSF6 defines a conserved capsid interface that modulates HIV-1 replication
Structural highlights
FunctionPublication Abstract from PubMedThe HIV-1 genome enters cells inside a shell comprised of capsid (CA) protein. Variation in CA sequence alters HIV-1 infectivity and escape from host restriction factors. However, apart from the Cyclophilin A-binding loop, CA has no known interfaces with which to interact with cellular cofactors. Here we describe a novel protein-protein interface in the N-terminal domain of HIV-1 CA, determined by X-ray crystallography, which mediates both viral restriction and host cofactor dependence. The interface is highly conserved across lentiviruses and is accessible in the context of a hexameric lattice. Mutation of the interface prevents binding to and restriction by CPSF6-358, a truncated cytosolic form of the RNA processing factor, cleavage and polyadenylation specific factor 6 (CPSF6). Furthermore, mutations that prevent CPSF6 binding also relieve dependence on nuclear entry cofactors TNPO3 and RanBP2. These results suggest that the HIV-1 capsid mediates direct host cofactor interactions to facilitate viral infection. CPSF6 Defines a Conserved Capsid Interface that Modulates HIV-1 Replication.,Price AJ, Fletcher AJ, Schaller T, Elliott T, Lee K, Kewalramani VN, Chin JW, Towers GJ, James LC PLoS Pathog. 2012 Aug;8(8):e1002896. Epub 2012 Aug 30. PMID:22956906[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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