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- | [[Image:3pzp.jpg|left|200px]] | |
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- | <!-- | + | ==Human DNA polymerase kappa extending opposite a cis-syn thymine dimer== |
- | The line below this paragraph, containing "STRUCTURE_3pzp", creates the "Structure Box" on the page.
| + | <StructureSection load='3pzp' size='340' side='right'caption='[[3pzp]], [[Resolution|resolution]] 3.34Å' scene=''> |
- | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
- | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[3pzp]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PZP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PZP FirstGlance]. <br> |
- | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.336Å</td></tr> |
- | --> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTP:2-DEOXYADENOSINE+5-TRIPHOSPHATE'>DTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TTD:CIS-SYN+CYCLOBUTANE+THYMINE+DIMER'>TTD</scene></td></tr> |
- | {{STRUCTURE_3pzp| PDB=3pzp | SCENE= }}
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3pzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pzp OCA], [https://pdbe.org/3pzp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pzp RCSB], [https://www.ebi.ac.uk/pdbsum/3pzp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pzp ProSAT]</span></td></tr> |
| + | </table> |
| + | == Function == |
| + | [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> |
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- | ===Human DNA polymerase kappa extending opposite a cis-syn thymine dimer=== | + | ==See Also== |
- | | + | *[[DNA polymerase 3D structures|DNA polymerase 3D structures]] |
- | | + | == References == |
- | <!--
| + | <references/> |
- | The line below this paragraph, {{ABSTRACT_PUBMED_21354175}}, adds the Publication Abstract to the page
| + | __TOC__ |
- | (as it appears on PubMed at http://www.pubmed.gov), where 21354175 is the PubMed ID number.
| + | </StructureSection> |
- | -->
| + | |
- | {{ABSTRACT_PUBMED_21354175}}
| + | |
- | | + | |
- | ==About this Structure==
| + | |
- | [[3pzp]] is a 6 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=3PZP OCA]. | + | |
- | | + | |
- | ==Reference== | + | |
- | <ref group="xtra">PMID:021354175</ref><references group="xtra"/> | + | |
- | [[Category: DNA-directed DNA polymerase]]
| + | |
| [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
- | [[Category: Aggarwal, A K.]] | + | [[Category: Large Structures]] |
- | [[Category: Carpio, R Vasquez-Del.]] | + | [[Category: Aggarwal AK]] |
- | [[Category: Johnson, R E.]] | + | [[Category: Johnson RE]] |
- | [[Category: Lone, S.]] | + | [[Category: Lone S]] |
- | [[Category: Prakash, L.]] | + | [[Category: Prakash L]] |
- | [[Category: Prakash, S.]] | + | [[Category: Prakash S]] |
- | [[Category: Silverstein, T D.]] | + | [[Category: Silverstein TD]] |
- | [[Category: Dna binding nucleotide binding magnesium binding]] | + | [[Category: Vasquez-Del Carpio R]] |
- | [[Category: Dna nucleotidyltransferase]]
| + | |
- | [[Category: Nucleus]]
| + | |
- | [[Category: Transferase-dna complex]]
| + | |
| Structural highlights
Function
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.[1] [2] [3] [4] [5] [6] [7]
See Also
References
- ↑ Ogi T, Kato T Jr, Kato T, Ohmori H. Mutation enhancement by DINB1, a mammalian homologue of the Escherichia coli mutagenesis protein dinB. Genes Cells. 1999 Nov;4(11):607-18. PMID:10620008
- ↑ Gerlach VL, Feaver WJ, Fischhaber PL, Friedberg EC. Purification and characterization of pol kappa, a DNA polymerase encoded by the human DINB1 gene. J Biol Chem. 2001 Jan 5;276(1):92-8. PMID:11024016 doi:http://dx.doi.org/10.1074/jbc.M004413200
- ↑ Fischhaber PL, Gerlach VL, Feaver WJ, Hatahet Z, Wallace SS, Friedberg EC. Human DNA polymerase kappa bypasses and extends beyond thymine glycols during translesion synthesis in vitro, preferentially incorporating correct nucleotides. J Biol Chem. 2002 Oct 4;277(40):37604-11. Epub 2002 Jul 26. PMID:12145297 doi:10.1074/jbc.M206027200
- ↑ Haracska L, Prakash L, Prakash S. Role of human DNA polymerase kappa as an extender in translesion synthesis. Proc Natl Acad Sci U S A. 2002 Dec 10;99(25):16000-5. Epub 2002 Nov 20. PMID:12444249 doi:10.1073/pnas.252524999
- ↑ Wolfle WT, Washington MT, Prakash L, Prakash S. Human DNA polymerase kappa uses template-primer misalignment as a novel means for extending mispaired termini and for generating single-base deletions. Genes Dev. 2003 Sep 1;17(17):2191-9. PMID:12952891 doi:http://dx.doi.org/10.1101/gad.1108603
- ↑ Haracska L, Prakash L, Prakash S. A mechanism for the exclusion of low-fidelity human Y-family DNA polymerases from base excision repair. Genes Dev. 2003 Nov 15;17(22):2777-85. PMID:14630940 doi:10.1101/gad.1146103
- ↑ Yasui M, Suzuki N, Miller H, Matsuda T, Matsui S, Shibutani S. Translesion synthesis past 2'-deoxyxanthosine, a nitric oxide-derived DNA adduct, by mammalian DNA polymerases. J Mol Biol. 2004 Nov 26;344(3):665-74. PMID:15533436 doi:S0022-2836(04)01222-7
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