4b4n: Difference between revisions

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<StructureSection load='4b4n' size='340' side='right'caption='[[4b4n]], [[Resolution|resolution]] 1.81&Aring;' scene=''>
<StructureSection load='4b4n' size='340' side='right'caption='[[4b4n]], [[Resolution|resolution]] 1.81&Aring;' 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/9hiv1 9hiv1] and [https://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 [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='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/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>   
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 09:59, 31 August 2022

CPSF6 defines a conserved capsid interface that modulates HIV-1 replicationCPSF6 defines a conserved capsid interface that modulates HIV-1 replication

Structural highlights

4b4n is a 2 chain structure with sequence from 9hiv1 and Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 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[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Ruegsegger U, Blank D, Keller W. Human pre-mRNA cleavage factor Im is related to spliceosomal SR proteins and can be reconstituted in vitro from recombinant subunits. Mol Cell. 1998 Jan;1(2):243-53. PMID:9659921
  2. ↑ Ruegsegger U, Beyer K, Keller W. Purification and characterization of human cleavage factor Im involved in the 3' end processing of messenger RNA precursors. J Biol Chem. 1996 Mar 15;271(11):6107-13. PMID:8626397
  3. ↑ Brown KM, Gilmartin GM. A mechanism for the regulation of pre-mRNA 3' processing by human cleavage factor Im. Mol Cell. 2003 Dec;12(6):1467-76. PMID:14690600
  4. ↑ Kim S, Yamamoto J, Chen Y, Aida M, Wada T, Handa H, Yamaguchi Y. Evidence that cleavage factor Im is a heterotetrameric protein complex controlling alternative polyadenylation. Genes Cells. 2010 Sep 1;15(9):1003-13. doi: 10.1111/j.1365-2443.2010.01436.x., Epub 2010 Jul 29. PMID:20695905 doi:10.1111/j.1365-2443.2010.01436.x
  5. ↑ Yang Q, Coseno M, Gilmartin GM, Doublie S. Crystal Structure of a Human Cleavage Factor CFI(m)25/CFI(m)68/RNA Complex Provides an Insight into Poly(A) Site Recognition and RNA Looping. Structure. 2011 Feb 2. PMID:21295486 doi:10.1016/j.str.2010.12.021
  6. ↑ 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

4b4n, resolution 1.81Å

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