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| - | {{Seed}} |  | 
| - | [[Image:2pqa.png|left|200px]] |  | 
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| - | <!--
 | + | ==Crystal Structure of Full-length Human RPA 14/32 Heterodimer== | 
| - | The line below this paragraph, containing "STRUCTURE_2pqa", creates the "Structure Box" on the page.
 | + | <StructureSection load='2pqa' size='340' side='right'caption='[[2pqa]], [[Resolution|resolution]] 2.50Å' scene=''> | 
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet) 
 | + | == Structural highlights == | 
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
 | + | <table><tr><td colspan='2'>[[2pqa]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PQA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PQA FirstGlance]. <br> | 
| - | or leave the SCENE parameter empty for the default display.
 | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</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=2pqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pqa OCA], [https://pdbe.org/2pqa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pqa RCSB], [https://www.ebi.ac.uk/pdbsum/2pqa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pqa ProSAT]</span></td></tr> | 
| - | {{STRUCTURE_2pqa|  PDB=2pqa  |  SCENE=  }} 
 | + | </table> | 
| - |   | + | == Function == | 
| - | ===Crystal Structure of Full-length Human RPA 14/32 Heterodimer===
 | + | [https://www.uniprot.org/uniprot/RFA2_HUMAN RFA2_HUMAN] Required for DNA recombination, repair and replication. The activity of RP-A is mediated by single-stranded DNA binding and protein interactions. Required for the efficient recruitment of the DNA double-strand break repair factor RAD51 to chromatin in response to DNA damage.<ref>PMID:15205463</ref> <ref>PMID:19116208</ref> <ref>PMID:19996105</ref> <ref>PMID:20154705</ref>   Functions as component of the alternative replication protein A complex (aRPA). aRPA binds single-stranded DNA and probably plays a role in DNA repair; it does not support chromosomal DNA replication and cell cycle progression through S-phase. In vitro, aRPA cannot promote efficient priming by DNA polymerase alpha but supports DNA polymerase delta synthesis in the presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange.<ref>PMID:15205463</ref> <ref>PMID:19116208</ref> <ref>PMID:19996105</ref> <ref>PMID:20154705</ref>  | 
| - |   | + | == Evolutionary Conservation == | 
| - |   | + | [[Image:Consurf_key_small.gif|200px|right]] | 
| - | <!--  | + | Check<jmol> | 
| - | The line below this paragraph,{{ABSTRACT_PUBMED_17976647}}, adds the Publication Abstract to the page 
 | + |   <jmolCheckbox> | 
| - | (as it appears on PubMed at http://www.pubmed.gov), where 17976647 is the PubMed ID number.
 | + |     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pq/2pqa_consurf.spt"</scriptWhenChecked> | 
| - | -->
 | + |     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | 
| - | {{ABSTRACT_PUBMED_17976647}}
 | + |     <text>to colour the structure by Evolutionary Conservation</text> | 
| - |   | + |   </jmolCheckbox> | 
| - | ==About this Structure== | + | </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=2pqa ConSurf]. | 
| - | 2PQA is a 4chains structureof sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PQA OCA].
 | + | <div style="clear:both"></div> | 
| - |   | + | == References == | 
| - | ==Reference== | + | <references/> | 
| - | <ref group="xtra">PMID:17976647</ref><references group="xtra"/> | + | __TOC__ | 
|  | + | </StructureSection> | 
|  | [[Category: Homo sapiens]] |  | [[Category: Homo sapiens]] | 
| - | [[Category: Borgstahl, G E.]] | + | [[Category: Large Structures]] | 
| - | [[Category: Deng, X.]] | + | [[Category: Borgstahl GE]] | 
| - | [[Category: Ob-fold]] | + | [[Category: Deng X]] | 
| - | [[Category: Replication]]
 | + |  | 
| - | [[Category: Rpa14/32]]
 | + |  | 
| - | [[Category: Ssdna binding protein]]
 | + |  | 
| - |   | + |  | 
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 13:13:37 2009''
 | + |  | 
|  |   Structural highlights   Function RFA2_HUMAN Required for DNA recombination, repair and replication. The activity of RP-A is mediated by single-stranded DNA binding and protein interactions. Required for the efficient recruitment of the DNA double-strand break repair factor RAD51 to chromatin in response to DNA damage.[1] [2] [3] [4]   Functions as component of the alternative replication protein A complex (aRPA). aRPA binds single-stranded DNA and probably plays a role in DNA repair; it does not support chromosomal DNA replication and cell cycle progression through S-phase. In vitro, aRPA cannot promote efficient priming by DNA polymerase alpha but supports DNA polymerase delta synthesis in the presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange.[5] [6] [7] [8] 
   Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
   References ↑ Weisshart K, Pestryakov P, Smith RW, Hartmann H, Kremmer E, Lavrik O, Nasheuer HP. Coordinated regulation of replication protein A activities by its subunits p14 and p32. J Biol Chem. 2004 Aug 20;279(34):35368-76. Epub 2004 Jun 17. PMID:15205463 doi:10.1074/jbc.M403825200↑ Mason AC, Haring SJ, Pryor JM, Staloch CA, Gan TF, Wold MS. An alternative form of replication protein a prevents viral replication in vitro. J Biol Chem. 2009 Feb 20;284(8):5324-31. doi: 10.1074/jbc.M808963200. Epub 2008, Dec 29. PMID:19116208 doi:10.1074/jbc.M808963200↑ Kemp MG, Mason AC, Carreira A, Reardon JT, Haring SJ, Borgstahl GE, Kowalczykowski SC, Sancar A, Wold MS. An alternative form of replication protein a expressed in normal human tissues supports DNA repair. J Biol Chem. 2010 Feb 12;285(7):4788-97. doi: 10.1074/jbc.M109.079418. Epub 2009 , Dec 7. PMID:19996105 doi:10.1074/jbc.M109.079418↑ Lee DH, Pan Y, Kanner S, Sung P, Borowiec JA, Chowdhury D. A PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA repair via homologous recombination. Nat Struct Mol Biol. 2010 Mar;17(3):365-72. doi: 10.1038/nsmb.1769. Epub 2010 Feb, 14. PMID:20154705 doi:10.1038/nsmb.1769↑ Weisshart K, Pestryakov P, Smith RW, Hartmann H, Kremmer E, Lavrik O, Nasheuer HP. Coordinated regulation of replication protein A activities by its subunits p14 and p32. J Biol Chem. 2004 Aug 20;279(34):35368-76. Epub 2004 Jun 17. PMID:15205463 doi:10.1074/jbc.M403825200↑ Mason AC, Haring SJ, Pryor JM, Staloch CA, Gan TF, Wold MS. An alternative form of replication protein a prevents viral replication in vitro. J Biol Chem. 2009 Feb 20;284(8):5324-31. doi: 10.1074/jbc.M808963200. Epub 2008, Dec 29. PMID:19116208 doi:10.1074/jbc.M808963200↑ Kemp MG, Mason AC, Carreira A, Reardon JT, Haring SJ, Borgstahl GE, Kowalczykowski SC, Sancar A, Wold MS. An alternative form of replication protein a expressed in normal human tissues supports DNA repair. J Biol Chem. 2010 Feb 12;285(7):4788-97. doi: 10.1074/jbc.M109.079418. Epub 2009 , Dec 7. PMID:19996105 doi:10.1074/jbc.M109.079418↑ Lee DH, Pan Y, Kanner S, Sung P, Borowiec JA, Chowdhury D. A PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA repair via homologous recombination. Nat Struct Mol Biol. 2010 Mar;17(3):365-72. doi: 10.1038/nsmb.1769. Epub 2010 Feb, 14. PMID:20154705 doi:10.1038/nsmb.1769
 
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