5l2x: Difference between revisions
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==Crystal structure of human PrimPol ternary complex== | |||
<StructureSection load='5l2x' size='340' side='right'caption='[[5l2x]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5l2x]] 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=5L2X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5L2X 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]] 2.2Å</td></tr> | |||
[[Category: | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5IU:5-IODO-2-DEOXYURIDINE-5-MONOPHOSPHATE'>5IU</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DDG:2,3-DIDEOXY-GUANOSINE-5-MONOPHOSPHATE'>DDG</scene>, <scene name='pdbligand=DTP:2-DEOXYADENOSINE+5-TRIPHOSPHATE'>DTP</scene></td></tr> | ||
[[Category: | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5l2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l2x OCA], [https://pdbe.org/5l2x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5l2x RCSB], [https://www.ebi.ac.uk/pdbsum/5l2x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5l2x ProSAT]</span></td></tr> | ||
[[Category: | </table> | ||
[[Category: Johnson | == Disease == | ||
[[Category: | [https://www.uniprot.org/uniprot/PRIPO_HUMAN PRIPO_HUMAN] The disease is caused by mutations affecting the gene represented in this entry. | ||
[[Category: Prakash | == Function == | ||
[[Category: Prakash | [https://www.uniprot.org/uniprot/PRIPO_HUMAN PRIPO_HUMAN] DNA primase and DNA polymerase able to initiate de novo DNA synthesis using dNTPs. Shows a high capacity to tolerate DNA damage lesions such as 8oxoG and abasic sites in DNA. Involved in translesion synthesis via its primase activity by mediating uninterrupted fork progression after programmed or damage-induced fork arrest and by reinitiating DNA synthesis after dNTP depletion. Required for mitochondrial DNA (mtDNA) synthesis, suggesting it may be involved in DNA tolerance during the replication of mitochondrial DNA. Has non-overlapping function with POLH.<ref>PMID:24126761</ref> <ref>PMID:24207056</ref> <ref>PMID:24240614</ref> <ref>PMID:24267451</ref> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Aggarwal AK]] | |||
[[Category: Gupta YK]] | |||
[[Category: Johnson RE]] | |||
[[Category: Malik R]] | |||
[[Category: Prakash L]] | |||
[[Category: Prakash S]] | |||
[[Category: Rajashankar KR]] | |||
[[Category: Rechkoblit O]] |
Latest revision as of 15:43, 6 March 2024
Crystal structure of human PrimPol ternary complexCrystal structure of human PrimPol ternary complex
Structural highlights
DiseasePRIPO_HUMAN The disease is caused by mutations affecting the gene represented in this entry. FunctionPRIPO_HUMAN DNA primase and DNA polymerase able to initiate de novo DNA synthesis using dNTPs. Shows a high capacity to tolerate DNA damage lesions such as 8oxoG and abasic sites in DNA. Involved in translesion synthesis via its primase activity by mediating uninterrupted fork progression after programmed or damage-induced fork arrest and by reinitiating DNA synthesis after dNTP depletion. Required for mitochondrial DNA (mtDNA) synthesis, suggesting it may be involved in DNA tolerance during the replication of mitochondrial DNA. Has non-overlapping function with POLH.[1] [2] [3] [4] References
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