9mj5
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Catalytic domain of human DNA polymerase alpha in complex with DNA and RPA== | |
- | + | <StructureSection load='9mj5' size='340' side='right'caption='[[9mj5]], [[Resolution|resolution]] 3.50Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[9mj5]] is a 6 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=9MJ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9MJ5 FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5Å</td></tr> | |
- | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DCP:2-DEOXYCYTIDINE-5-TRIPHOSPHATE'>DCP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=9mj5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9mj5 OCA], [https://pdbe.org/9mj5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9mj5 RCSB], [https://www.ebi.ac.uk/pdbsum/9mj5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9mj5 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/RFA3_HUMAN RFA3_HUMAN] Required for DNA recombination, repair and replication. The activity of RP-A is mediated by single-stranded DNA binding and protein interactions.<ref>PMID:19116208</ref> <ref>PMID:19996105</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:19116208</ref> <ref>PMID:19996105</ref> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Homo sapiens]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Babayeva ND]] | ||
+ | [[Category: Baranovskiy AG]] | ||
+ | [[Category: Morstadt LM]] | ||
+ | [[Category: Romero EE]] | ||
+ | [[Category: Tahirov TH]] |
Current revision
Catalytic domain of human DNA polymerase alpha in complex with DNA and RPA
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