3IN5
Structure of human DNA polymerase kappa inserting dATP opposite an 8-oxoG DNA lesion
Replaces: 3HEDSummary for 3IN5
Entry DOI | 10.2210/pdb3in5/pdb |
Related | 1T94 2OH2 |
Descriptor | DNA polymerase kappa, DNA (5'-D(*GP*G*GP*GP*GP*AP*AP*GP*GP*AP*CP*TP*(DOC))-3'), DNA (5'-D(*C*CP*TP*AP*(8OG)P*GP*AP*GP*TP*CP*CP*TP*TP*CP*CP*CP*CP*C)-3'), ... (6 entities in total) |
Functional Keywords | alternative splicing, dna damage, dna repair, dna replication, dna synthesis, dna-binding, dna-directed dna polymerase, magnesium, metal-binding, mutator protein, nucleotidyltransferase, nucleus, phosphoprotein, polymorphism, schiff base, transferase, zinc, zinc-finger, transferase-dna complex, transferase/dna |
Biological source | Homo sapiens (human) |
Cellular location | Nucleus: Q9UBT6 |
Total number of polymer chains | 6 |
Total formula weight | 136128.45 |
Authors | Silverstein, T.D.,Vasquez-Del Carpio, R.,Aggarwal, A.K. (deposition date: 2009-08-11, release date: 2009-09-08, Last modification date: 2023-09-06) |
Primary citation | Vasquez-Del Carpio, R.,Silverstein, T.D.,Lone, S.,Swan, M.K.,Choudhury, J.R.,Johnson, R.E.,Prakash, S.,Prakash, L.,Aggarwal, A.K. Structure of human DNA polymerase kappa inserting dATP opposite an 8-oxoG DNA lesion PLOS ONE, 4:e5766-e5766, 2009 Cited by PubMed Abstract: Oxygen-free radicals formed during normal aerobic cellular metabolism attack bases in DNA and 7,8-dihydro-8-oxoguanine (8-oxoG) is one of the major lesions formed. It is amongst the most mutagenic lesions in cells because of its dual coding potential, wherein 8-oxoG(syn) can pair with an A in addition to normal base pairing of 8-oxoG(anti) with a C. Human DNA polymerase kappa (Polkappa) is a member of the newly discovered Y-family of DNA polymerases that possess the ability to replicate through DNA lesions. To understand the basis of Polkappa's preference for insertion of an A opposite 8-oxoG lesion, we have solved the structure of Polkappa in ternary complex with a template-primer presenting 8-oxoG in the active site and with dATP as the incoming nucleotide. PubMed: 19492058DOI: 10.1371/journal.pone.0005766 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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