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==Solution structure of polymerase-interacting domain of human Rev1 in complex with translesional synthesis polymerase kappa==
==Solution structure of polymerase-interacting domain of human Rev1 in complex with translesional synthesis polymerase kappa==
<StructureSection load='2lsi' size='340' side='right'caption='[[2lsi]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''>
<StructureSection load='2lsi' size='340' side='right'caption='[[2lsi]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2lsi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LSI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LSI FirstGlance]. <br>
<table><tr><td colspan='2'>[[2lsi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LSI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LSI FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">REV1, REV1L ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
</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=2lsi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lsi OCA], [https://pdbe.org/2lsi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lsi RCSB], [https://www.ebi.ac.uk/pdbsum/2lsi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lsi ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </span></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=2lsi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lsi OCA], [https://pdbe.org/2lsi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lsi RCSB], [https://www.ebi.ac.uk/pdbsum/2lsi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lsi ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/REV1_HUMAN REV1_HUMAN]] 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:10536157</ref> <ref>PMID:10760286</ref> <ref>PMID:11278384</ref> <ref>PMID:11485998</ref> <ref>PMID:22266823</ref> [[https://www.uniprot.org/uniprot/POLK_HUMAN POLK_HUMAN]] 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.<ref>PMID:10620008</ref> <ref>PMID:11024016</ref> <ref>PMID:12145297</ref> <ref>PMID:12444249</ref> <ref>PMID:12952891</ref> <ref>PMID:14630940</ref> <ref>PMID:15533436</ref> 
[https://www.uniprot.org/uniprot/REV1_HUMAN REV1_HUMAN] 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:10536157</ref> <ref>PMID:10760286</ref> <ref>PMID:11278384</ref> <ref>PMID:11485998</ref> <ref>PMID:22266823</ref>  
 
==See Also==
*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: DNA-directed DNA polymerase]]
[[Category: Homo sapiens]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Choi, B]]
[[Category: Choi B]]
[[Category: Ko, J]]
[[Category: Ko J]]
[[Category: Liu, D]]
[[Category: Liu D]]
[[Category: Ryu, K]]
[[Category: Ryu K]]
[[Category: Polymerase kappa]]
[[Category: Polymerase-interacting domain]]
[[Category: Rev1]]
[[Category: Rev1-interacting motif]]
[[Category: Transferase]]

Revision as of 11:15, 15 February 2023

Solution structure of polymerase-interacting domain of human Rev1 in complex with translesional synthesis polymerase kappa

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