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| | <StructureSection load='4b4n' size='340' side='right'caption='[[4b4n]], [[Resolution|resolution]] 1.81Å' scene=''> | | <StructureSection load='4b4n' size='340' side='right'caption='[[4b4n]], [[Resolution|resolution]] 1.81Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4b4n]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/9hiv1 9hiv1] and [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4B4N FirstGlance]. <br> | + | <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='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=4b4n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b4n OCA], [http://pdbe.org/4b4n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4b4n RCSB], [http://www.ebi.ac.uk/pdbsum/4b4n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4b4n ProSAT]</span></td></tr> | + | </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> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CPSF6_HUMAN CPSF6_HUMAN]] Component of the cleavage factor Im complex (CFIm) that plays a key role in pre-mRNA 3'-processing. Involved in association with NUDT21/CPSF5 in pre-MRNA 3'-end poly(A) site cleavage and poly(A) addition. CPSF6 binds to cleavage and polyadenylation RNA substrates and promotes RNA looping.<ref>PMID:9659921</ref> <ref>PMID:8626397</ref> <ref>PMID:14690600</ref> <ref>PMID:20695905</ref> <ref>PMID:21295486</ref> | + | [https://www.uniprot.org/uniprot/A9PKC6_9HIV1 A9PKC6_9HIV1] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | + | [[Category: Human immunodeficiency virus 1]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: James, L C]] | + | [[Category: James LC]] |
| - | [[Category: Price, A J]] | + | [[Category: Price AJ]] |
| - | [[Category: Cyclophilin]]
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| - | [[Category: Hiv-1]]
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| - | [[Category: Viral protein-rna binding protein complex]]
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| Structural highlights
Function
A9PKC6_9HIV1
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Price AJ, Fletcher AJ, Schaller T, Elliott T, Lee K, Kewalramani VN, Chin JW, Towers GJ, James LC. CPSF6 Defines a Conserved Capsid Interface that Modulates HIV-1 Replication. PLoS Pathog. 2012 Aug;8(8):e1002896. Epub 2012 Aug 30. PMID:22956906 doi:http://dx.doi.org/10.1371/journal.ppat.1002896
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