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4u6p
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(Difference between revisions)
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| - | ''' | + | ==Structural mechanism of error-free bypass of major benzo[a]pyrene adduct by human polymerase kappa== |
| - | + | <StructureSection load='4u6p' size='340' side='right' caption='[[4u6p]], [[Resolution|resolution]] 2.59Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4u6p]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U6P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4U6P FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DCT:2,3-DIDEOXYCYTIDINE+5-TRIPHOSPHATE'>DCT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> | |
| - | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4u7c|4u7c]]</td></tr> | |
| - | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </span></td></tr> | |
| - | [[Category: | + | <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=4u6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u6p OCA], [http://pdbe.org/4u6p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4u6p RCSB], [http://www.ebi.ac.uk/pdbsum/4u6p PDBsum]</span></td></tr> |
| - | [[Category: Jha, V | + | </table> |
| + | == Function == | ||
| + | [[http://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> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: DNA-directed DNA polymerase]] | ||
| + | [[Category: Jha, V K]] | ||
[[Category: Ling, H]] | [[Category: Ling, H]] | ||
| + | [[Category: Dna damage tolerance]] | ||
| + | [[Category: Dna replication]] | ||
| + | [[Category: Environment pollution]] | ||
| + | [[Category: Polymerase kappa]] | ||
| + | [[Category: Transferase-dna complex]] | ||
Revision as of 02:26, 28 January 2016
Structural mechanism of error-free bypass of major benzo[a]pyrene adduct by human polymerase kappa
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