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| {{STRUCTURE_3ggr| PDB=3ggr | SCENE= }}
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| ===Crystal Structure of the Human Rad9-Hus1-Rad1 complex===
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| {{ABSTRACT_PUBMED_19535328}}
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| ==Function== | | ==Crystal Structure of the Human Rad9-Hus1-Rad1 complex== |
| [[http://www.uniprot.org/uniprot/RAD9A_HUMAN RAD9A_HUMAN]] Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase. RAD9A possesses 3'->5' double stranded DNA exonuclease activity. Its phosphorylation by PRKCD may be required for the formation of the 9-1-1 complex.<ref>PMID:10713044</ref> <ref>PMID:21659603</ref> [[http://www.uniprot.org/uniprot/RAD1_HUMAN RAD1_HUMAN]] Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase. Isoform 1 possesses 3'->5' double stranded DNA exonuclease activity.<ref>PMID:9660799</ref> <ref>PMID:21659603</ref> [[http://www.uniprot.org/uniprot/HUS1_HUMAN HUS1_HUMAN]] Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase.<ref>PMID:21659603</ref> | | <StructureSection load='3ggr' size='340' side='right'caption='[[3ggr]], [[Resolution|resolution]] 3.20Å' scene=''> |
| | | == Structural highlights == |
| ==About this Structure==
| | <table><tr><td colspan='2'>[[3ggr]] is a 3 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=3GGR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GGR FirstGlance]. <br> |
| [[3ggr]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GGR OCA].
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2Å</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=3ggr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ggr OCA], [https://pdbe.org/3ggr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ggr RCSB], [https://www.ebi.ac.uk/pdbsum/3ggr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ggr ProSAT]</span></td></tr> |
| ==Reference==
| | </table> |
| <ref group="xtra">PMID:019535328</ref><references group="xtra"/><references/> | | == Function == |
| [[Category: Exodeoxyribonuclease III]] | | [https://www.uniprot.org/uniprot/RAD9A_HUMAN RAD9A_HUMAN] Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase. RAD9A possesses 3'->5' double stranded DNA exonuclease activity. Its phosphorylation by PRKCD may be required for the formation of the 9-1-1 complex.<ref>PMID:10713044</ref> <ref>PMID:21659603</ref> |
| [[Category: Human]] | | == Evolutionary Conservation == |
| [[Category: Bai, L.]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| [[Category: Hang, H Y.]] | | Check<jmol> |
| [[Category: Jiang, T.]] | | <jmolCheckbox> |
| [[Category: Xu, M.]] | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gg/3ggr_consurf.spt"</scriptWhenChecked> |
| [[Category: Cell cycle]]
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| [[Category: Dna damage]]
| | <text>to colour the structure by Evolutionary Conservation</text> |
| [[Category: Dna repair]]
| | </jmolCheckbox> |
| [[Category: Exonuclease]]
| | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ggr ConSurf]. |
| [[Category: Hydrolase]]
| | <div style="clear:both"></div> |
| [[Category: Nuclease]]
| | == References == |
| [[Category: Nucleus]]
| | <references/> |
| [[Category: Phosphoprotein]]
| | __TOC__ |
| [[Category: Protein-protein complex]]
| | </StructureSection> |
| | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] |
| | [[Category: Bai L]] |
| | [[Category: Hang HY]] |
| | [[Category: Jiang T]] |
| | [[Category: Xu M]] |
