4b4n: Difference between revisions
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==CPSF6 defines a conserved capsid interface that modulates HIV-1 replication== | ==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=''> | <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 [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> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: James, L C]] | [[Category: James, L C]] | ||
[[Category: Price, A J]] | [[Category: Price, A J]] | ||
Revision as of 16:04, 13 March 2019
CPSF6 defines a conserved capsid interface that modulates HIV-1 replicationCPSF6 defines a conserved capsid interface that modulates HIV-1 replication
Structural highlights
Function[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.[1] [2] [3] [4] [5] Publication 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[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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