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''' | ==Crystal structure of human PCNA in complex with p15 peptide== | ||
<StructureSection load='4d2g' size='340' side='right' caption='[[4d2g]], [[Resolution|resolution]] 2.65Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4d2g]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D2G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D2G 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=4d2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d2g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4d2g RCSB], [http://www.ebi.ac.uk/pdbsum/4d2g PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[Category: | [[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> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bernardo, P]] | |||
[[Category: Blanco, F J]] | |||
[[Category: Castillo, F]] | |||
[[Category: Cordeiro, T N]] | |||
[[Category: DeBiasio, A]] | |||
[[Category: Diercks, T]] | |||
[[Category: Ibanez, A]] | [[Category: Ibanez, A]] | ||
[[Category: Lelli, M]] | [[Category: Lelli, M]] | ||
[[Category: | [[Category: Luque, I]] | ||
[[Category: | [[Category: Merino, N]] | ||
[[Category: Molina, R]] | [[Category: Molina, R]] | ||
[[Category: | [[Category: Montoya, G]] | ||
[[Category: | [[Category: Mortuza, G]] | ||
[[Category: Villate, M]] | [[Category: Villate, M]] | ||
[[Category: | [[Category: Transcription]] | ||
Revision as of 15:09, 18 March 2015
Crystal structure of human PCNA in complex with p15 peptideCrystal structure of human PCNA in complex with p15 peptide
Structural highlights
Function[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.[1] [2] References
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