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1vyj
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1vyj]] is a 12 chain structure with sequence 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=1VYJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VYJ FirstGlance]. <br> | <table><tr><td colspan='2'>[[1vyj]] is a 12 chain structure with sequence 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=1VYJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VYJ FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1axc|1axc]], [[1u76|1u76]], [[1u7b|1u7b]], [[1vym|1vym]], [[1w60|1w60]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1axc|1axc]], [[1u76|1u76]], [[1u7b|1u7b]], [[1vym|1vym]], [[1w60|1w60]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vyj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vyj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1vyj RCSB], [http://www.ebi.ac.uk/pdbsum/1vyj 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=1vyj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vyj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1vyj RCSB], [http://www.ebi.ac.uk/pdbsum/1vyj PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PCNA_HUMAN PCNA_HUMAN]] Auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Induces a robust stimulatory effect on the 3'-5' exonuclease and 3'-phosphodiesterase, but not apurinic-apyrimidinic (AP) endonuclease, APEX2 activities. Has to be loaded onto DNA in order to be able to stimulate APEX2. Plays a key role in DNA damage response (DDR) by being conveniently positioned at the replication fork to coordinate DNA replication with DNA repair and DNA damage tolerance pathways. Acts as a loading platform to recruit DDR proteins that allow completion of DNA replication after DNA damage and promote postreplication repair: Monoubiquitinated PCNA leads to recruitment of translesion (TLS) polymerases, while 'Lys-63'-linked polyubiquitination of PCNA is involved in error-free pathway and employs recombination mechanisms to synthesize across the lesion.<ref>PMID:19443450</ref> <ref>PMID:18719106</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Fischer, P | + | [[Category: Fischer, P]] |
| - | [[Category: Kontopidis, G | + | [[Category: Kontopidis, G]] |
| - | [[Category: Lane, D | + | [[Category: Lane, D]] |
| - | [[Category: Mcinnes, C | + | [[Category: Mcinnes, C]] |
| - | [[Category: Taylor, P | + | [[Category: Taylor, P]] |
| - | [[Category: Walkinshaw, M D | + | [[Category: Walkinshaw, M D]] |
| - | [[Category: Wu, S | + | [[Category: Wu, S]] |
| - | [[Category: Zheleva, D | + | [[Category: Zheleva, D]] |
[[Category: Dna]] | [[Category: Dna]] | ||
[[Category: Dna replication]] | [[Category: Dna replication]] | ||
Revision as of 07:22, 25 December 2014
STRUCTURAL AND BIOCHEMICAL STUDIES OF HUMAN PCNA COMPLEXES PROVIDE THE BASIS FOR ASSOCIATION WITH CDK/CYCLIN AND RATIONALE FOR INHIBITOR DESIGN
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