4lwc

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<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=4lwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lwc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lwc RCSB], [http://www.ebi.ac.uk/pdbsum/4lwc PDBsum]</span></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=4lwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lwc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lwc RCSB], [http://www.ebi.ac.uk/pdbsum/4lwc PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/RFA1_HUMAN RFA1_HUMAN]] Plays an essential role in several cellular processes in DNA metabolism including replication, recombination and DNA repair. Binds and subsequently stabilizes single-stranded DNA intermediates and thus prevents complementary DNA from reannealing.<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>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 20:10, 24 December 2014

Fragment-Based Discovery of a Potent Inhibitor of Replication Protein A Protein-Protein Interactions

4lwc, resolution 1.61Å

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