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| {{STRUCTURE_4fjo| PDB=4fjo | SCENE= }}
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| ===Structure of the Rev1 CTD-Rev3/7-Pol kappa RIR complex===
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| {{ABSTRACT_PUBMED_22859295}}
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| ==Function== | | ==Structure of the Rev1 CTD-Rev3/7-Pol kappa RIR complex== |
| [[http://www.uniprot.org/uniprot/DPOLZ_MOUSE DPOLZ_MOUSE]] Interacts with MAD2L2 to form the error prone DNA polymerase zeta involved in translesion DNA synthesis (By similarity). [[http://www.uniprot.org/uniprot/REV1_MOUSE REV1_MOUSE]] Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents.<ref>PMID:11711549</ref> [[http://www.uniprot.org/uniprot/MD2L2_MOUSE MD2L2_MOUSE]] Adapter protein able to interact with different proteins and involved in different biological processes. Mediates the interaction between the error-prone DNA polymerase zeta catalytic subunit REV3L and the inserter polymerase REV1, thereby mediating the second polymerase switching in translesion DNA synthesis. Translesion DNA synthesis releases the replication blockade of replicative polymerases, stalled in presence of DNA lesions. May also regulate another aspect of cellular response to DNA damage through regulation of the JNK-mediated phosphorylation and activation of the transcriptional activator ELK1. Inhibits the FZR1- and probably CDC20-mediated activation of the anaphase promoting complex APC thereby regulating progression through the cell cycle. Regulates TCF7L2-mediated gene transcription and may play a role in epithelial-mesenchymal transdifferentiation (By similarity). [[http://www.uniprot.org/uniprot/POLK_MOUSE POLK_MOUSE]] DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Depending on the context, it inserts the correct base, but causes frequent base transitions, transversions and frameshifts. Lacks 3'-5' proofreading exonuclease activity. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity (By similarity).<ref>PMID:12432099</ref> | | <StructureSection load='4fjo' size='340' side='right'caption='[[4fjo]], [[Resolution|resolution]] 2.72Å' scene=''> |
| | == Structural highlights == |
| | <table><tr><td colspan='2'>[[4fjo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FJO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FJO FirstGlance]. <br> |
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.718Å</td></tr> |
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=4fjo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fjo OCA], [https://pdbe.org/4fjo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fjo RCSB], [https://www.ebi.ac.uk/pdbsum/4fjo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fjo ProSAT]</span></td></tr> |
| | </table> |
| | == Function == |
| | [https://www.uniprot.org/uniprot/REV1_MOUSE REV1_MOUSE] Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents.<ref>PMID:11711549</ref> |
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| ==About this Structure== | | ==See Also== |
| [[4fjo]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FJO OCA]. | | *[[DNA polymerase 3D structures|DNA polymerase 3D structures]] |
| | | == References == |
| ==Reference== | | <references/> |
| <ref group="xtra">PMID:022859295</ref><references group="xtra"/><references/>
| | __TOC__ |
| [[Category: DNA-directed DNA polymerase]] | | </StructureSection> |
| | [[Category: Large Structures]] |
| [[Category: Mus musculus]] | | [[Category: Mus musculus]] |
| [[Category: Lee, C J.]] | | [[Category: Lee C-J]] |
| [[Category: Wojtaszek, Jessica]] | | [[Category: Wojtaszek J]] |
| [[Category: Zhou, P.]] | | [[Category: Zhou P]] |
| [[Category: Transferase -dna binding protein complex]]
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| [[Category: Transferase-dna binding protein complex]]
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| [[Category: Translesion synthesis]]
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