3ja9
From Proteopedia
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| - | ''' | + | ==Structure of native human PCNA== |
| + | <StructureSection load='3ja9' size='340' side='right' caption='[[3ja9]], [[Resolution|resolution]] 22.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3ja9]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JA9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3JA9 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=3ja9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ja9 OCA], [http://pdbe.org/3ja9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ja9 RCSB], [http://www.ebi.ac.uk/pdbsum/3ja9 PDBsum]</span></td></tr> | ||
| + | </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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Translesion synthesis (TLS) is the mechanism by which DNA polymerases replicate through unrepaired DNA lesions. TLS is activated by monoubiquitination of the homotrimeric proliferating cell nuclear antigen (PCNA) at lysine-164, followed by the switch from replicative to specialized polymerases at DNA damage sites. Pol eta belongs to the Y-Family of specialized polymerases that can efficiently bypass UV-induced lesions. Like other members of the Y-Family polymerases, its recruitment to the damaged sites is mediated by the interaction with monoubiquitinated PCNA (Ub-PCNA) via its ubiquitin-binding domain and non-canonical PCNA-interacting motif in the C-terminal region. The structural determinants underlying the direct recognition of Ub-PCNA by Pol eta, or Y-Family polymerases in general, remain largely unknown. Here we report a structure of the Ub-PCNA/Pol eta complex bound to DNA determined by single-particle electron microscopy (EM). The overall obtained structure resembles that of the editing PCNA/PolB complex. Analysis of the map revealed the conformation of ubiquitin that binds the C-terminal domain of Pol eta. Our present study suggests that the Ub-PCNA/Pol eta interaction requires the formation of a structured binding interface, which is dictated by the inherent flexibility of Ub-PCNA. | ||
| - | + | Molecular architecture of the Ub-PCNA/Pol eta complex bound to DNA.,Lau WC, Li Y, Zhang Q, Huen MS Sci Rep. 2015 Oct 27;5:15759. doi: 10.1038/srep15759. PMID:26503230<ref>PMID:26503230</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3ja9" style="background-color:#fffaf0;"></div> | |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Huen, M S.Y]] | ||
| + | [[Category: Lau, W C.Y]] | ||
[[Category: Li, Y]] | [[Category: Li, Y]] | ||
| - | [[Category: Huen, M.S.Y]] | ||
| - | [[Category: Lau, W.C.Y]] | ||
[[Category: Zhang, Q]] | [[Category: Zhang, Q]] | ||
| + | [[Category: Dna]] | ||
| + | [[Category: Dna binding protein]] | ||
| + | [[Category: Dna-binding systemic lupus erythematosus]] | ||
| + | [[Category: Oncogene]] | ||
| + | [[Category: Processivity]] | ||
| + | [[Category: Replication]] | ||
Revision as of 13:42, 9 December 2015
Structure of native human PCNA
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