3g65 - Revision history

OCA at 07:00, 6 September 2023

OCA — Wed, 06 Sep 2023 07:00:04 GMT

←Older revision		Revision as of 07:00, 6 September 2023
Line 3:		Line 3:
	<StructureSection load='3g65' size='340' side='right'caption='[[3g65]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='3g65' size='340' side='right'caption='[[3g65]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3g65]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G65 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G65 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3g65]] 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=3G65 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G65 FirstGlance]. <br>
-	</td></tr><tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>RAD9, RAD9A ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=9606 HUMAN]), RAD1, REC1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), HUS1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.9Å</td></tr>
-	~~<tr id='activity'><td class~~="~~sblockLbl~~">~~<b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>~~[~~https://en.wikipedia.org/wiki/Exodeoxyribonuclease_III Exodeoxyribonuclease III~~]~~, with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.11.~~2 3.~~1.11.2] </span>~~</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=3g65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g65 OCA], [https://pdbe.org/3g65 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g65 RCSB], [https://www.ebi.ac.uk/pdbsum/3g65 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g65 ProSAT]</span></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=3g65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g65 OCA], [https://pdbe.org/3g65 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g65 RCSB], [https://www.ebi.ac.uk/pdbsum/3g65 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g65 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[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> [[https://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> [[https://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>	+	[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>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Exodeoxyribonuclease III]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Dore~~, A S~~]]	+	[[Category: Dore AS]]
-	[[Category: Kilkenny~~, M L~~]]	+	[[Category: Kilkenny ML]]
-	[[Category: Pearl~~, L H~~]]	+	[[Category: Pearl LH]]
-	[[Category: Rzechorzek~~, N J]]~~	+	[[Category: Rzechorzek NJ]]
-	~~[[Category: Cell cycle]]~~	+
-	~~[[Category: Dna binding clamp]]~~	+
-	~~[[Category: Dna damage]]~~	+
-	~~[[Category: Dna repair]]~~	+
-	~~[[Category: Exonuclease]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Nuclease]]~~	+
-	~~[[Category: Nucleus]]~~	+
-	~~[[Category: Pcna]]~~	+
-	~~[[Category: Phosphoprotein~~]]	+

OCA at 07:56, 9 March 2022

OCA — Wed, 09 Mar 2022 07:56:35 GMT

←Older revision		Revision as of 07:56, 9 March 2022
Line 1:		Line 1:

	==Crystal Structure of the Human Rad9-Rad1-Hus1 DNA Damage Checkpoint Complex==		==Crystal Structure of the Human Rad9-Rad1-Hus1 DNA Damage Checkpoint Complex==
-	<StructureSection load='3g65' size='340' side='right' caption='[[3g65]], [[Resolution\|resolution]] 2.90Å' scene=''>	+	<StructureSection load='3g65' size='340' side='right'caption='[[3g65]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3g65]] 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=3G65 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3G65 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3g65]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G65 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G65 FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">RAD9, RAD9A ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), RAD1, REC1 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), HUS1 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">RAD9, RAD9A ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), RAD1, REC1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), HUS1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Exodeoxyribonuclease_III Exodeoxyribonuclease III], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.11.2 3.1.11.2] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Exodeoxyribonuclease_III Exodeoxyribonuclease III], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.11.2 3.1.11.2] </span></td></tr>
-	<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=3g65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g65 OCA], [~~http~~://pdbe.org/3g65 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3g65 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3g65 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3g65 ProSAT]</span></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=3g65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g65 OCA], [https://pdbe.org/3g65 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g65 RCSB], [https://www.ebi.ac.uk/pdbsum/3g65 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g65 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~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/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> [[~~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>	+	[[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> [[https://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> [[https://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>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 35:		Line 35:
	[[Category: Exodeoxyribonuclease III]]		[[Category: Exodeoxyribonuclease III]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Dore, A S]]		[[Category: Dore, A S]]
	[[Category: Kilkenny, M L]]		[[Category: Kilkenny, M L]]

OCA at 08:05, 5 December 2018

OCA — Wed, 05 Dec 2018 08:05:20 GMT

←Older revision		Revision as of 08:05, 5 December 2018
Line 1:		Line 1:
		+
	==Crystal Structure of the Human Rad9-Rad1-Hus1 DNA Damage Checkpoint Complex==		==Crystal Structure of the Human Rad9-Rad1-Hus1 DNA Damage Checkpoint Complex==
	<StructureSection load='3g65' size='340' side='right' caption='[[3g65]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='3g65' size='340' side='right' caption='[[3g65]], [[Resolution\|resolution]] 2.90Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">RAD9, RAD9A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), RAD1, REC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), HUS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">RAD9, RAD9A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), RAD1, REC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), HUS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Exodeoxyribonuclease_III Exodeoxyribonuclease III], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.11.2 3.1.11.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Exodeoxyribonuclease_III Exodeoxyribonuclease III], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.11.2 3.1.11.2] </span></td></tr>
-	<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=3g65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g65 OCA], [http://pdbe.org/3g65 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3g65 RCSB], [http://www.ebi.ac.uk/pdbsum/3g65 PDBsum]</span></td></tr>	+	<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=3g65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g65 OCA], [http://pdbe.org/3g65 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3g65 RCSB], [http://www.ebi.ac.uk/pdbsum/3g65 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3g65 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 13:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g6/3g65_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g6/3g65_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 23:46, 7 February 2016

OCA — Sun, 07 Feb 2016 23:46:52 GMT

←Older revision		Revision as of 23:46, 7 February 2016
Line 2:		Line 2:
	<StructureSection load='3g65' size='340' side='right' caption='[[3g65]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='3g65' size='340' side='right' caption='[[3g65]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3g65]] is a 3 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=3G65 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3G65 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3g65]] 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=3G65 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3G65 FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">RAD9, RAD9A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~]), RAD1, REC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~]), HUS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">RAD9, RAD9A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), RAD1, REC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), HUS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Exodeoxyribonuclease_III Exodeoxyribonuclease III], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.11.2 3.1.11.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Exodeoxyribonuclease_III Exodeoxyribonuclease III], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.11.2 3.1.11.2] </span></td></tr>
-	<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=3g65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g65 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3g65 RCSB], [http://www.ebi.ac.uk/pdbsum/3g65 PDBsum]</span></td></tr>	+	<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=3g65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g65 OCA], [http://pdbe.org/3g65 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3g65 RCSB], [http://www.ebi.ac.uk/pdbsum/3g65 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 17:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</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/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</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=3g65 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 27:		Line 27:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 3g65" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
Line 32:		Line 33:
	</StructureSection>		</StructureSection>
	[[Category: Exodeoxyribonuclease III]]		[[Category: Exodeoxyribonuclease III]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Dore, A S]]		[[Category: Dore, A S]]
	[[Category: Kilkenny, M L]]		[[Category: Kilkenny, M L]]

OCA at 19:03, 24 December 2014

OCA — Wed, 24 Dec 2014 19:03:20 GMT

←Older revision		Revision as of 19:03, 24 December 2014
Line 7:		Line 7:
	<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=3g65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g65 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3g65 RCSB], [http://www.ebi.ac.uk/pdbsum/3g65 PDBsum]</span></td></tr>		<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=3g65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g65 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3g65 RCSB], [http://www.ebi.ac.uk/pdbsum/3g65 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[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/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> [[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>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 14:22, 18 December 2014

OCA — Thu, 18 Dec 2014 14:22:12 GMT

←Older revision		Revision as of 14:22, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3g65\| PDB=3g65 \| SCENE= }}~~	+	==Crystal Structure of the Human Rad9-Rad1-Hus1 DNA Damage Checkpoint Complex==
-	===Crystal Structure of the Human Rad9-Rad1-Hus1 DNA Damage Checkpoint Complex===	+	<StructureSection load='3g65' size='340' side='right' caption='[[3g65]], [[Resolution\|resolution]] 2.90Å' scene=''>
-	~~{{ABSTRACT_PUBMED_19446481}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3g65]] is a 3 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=3G65 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3G65 FirstGlance]. <br>
		+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">RAD9, RAD9A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), RAD1, REC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), HUS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Exodeoxyribonuclease_III Exodeoxyribonuclease III], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.11.2 3.1.11.2] </span></td></tr>
		+	<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=3g65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g65 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3g65 RCSB], [http://www.ebi.ac.uk/pdbsum/3g65 PDBsum]</span></td></tr>
		+	</table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g6/3g65_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</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/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Rad9, Rad1, and Hus1 form a heterotrimeric complex (9-1-1) that is loaded onto DNA at sites of DNA damage. DNA-loaded 9-1-1 activates signaling through the Chk1 arm of the DNA damage checkpoint response via recruitment and stimulation of ATR. Additionally, 9-1-1 may play a direct role in facilitating DNA damage repair via interaction with a number of DNA repair enzymes. We have now determined the crystal structure of the human 9-1-1 complex, revealing a toroidal structure with a similar architecture to the homotrimeric PCNA DNA-binding clamp. The structure explains the formation of a unique heterotrimeric arrangement and reveals significant differences among the three subunits in the sites implicated in binding to the clamp loader and to ligand proteins. Biochemical analysis reveals a single repair enzyme-binding site on 9-1-1 that can be blocked competitively by the PCNA-binding cell-cycle regulator p21(cip1/waf1).

-	~~==Function==~~	+	Crystal structure of the rad9-rad1-hus1 DNA damage checkpoint complex--implications for clamp loading and regulation.,Dore AS, Kilkenny ML, Rzechorzek NJ, Pearl LH Mol Cell. 2009 Jun 26;34(6):735-45. Epub 2009 May 14. PMID:19446481<ref>PMID:19446481</ref>
-	~~[[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/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> [[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>	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[3g65]] is~~ a ~~3 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=3G65 OCA].~~	+	</div>
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:019446481</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Exodeoxyribonuclease III]]		[[Category: Exodeoxyribonuclease III]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Dore, A S.]]	+	[[Category: Dore, A S]]
-	[[Category: Kilkenny, M L.]]	+	[[Category: Kilkenny, M L]]
-	[[Category: Pearl, L H.]]	+	[[Category: Pearl, L H]]
-	[[Category: Rzechorzek, N J.]]	+	[[Category: Rzechorzek, N J]]
	[[Category: Cell cycle]]		[[Category: Cell cycle]]
	[[Category: Dna binding clamp]]		[[Category: Dna binding clamp]]

OCA at 06:50, 29 September 2013

OCA — Sun, 29 Sep 2013 06:50:02 GMT

←Older revision		Revision as of 06:50, 29 September 2013
Line 1:		Line 1:
-	[[Image:3g65.png\|left\|200px]]
-
	{{STRUCTURE_3g65\| PDB=3g65 \| SCENE= }}		{{STRUCTURE_3g65\| PDB=3g65 \| SCENE= }}
-
	===Crystal Structure of the Human Rad9-Rad1-Hus1 DNA Damage Checkpoint Complex===		===Crystal Structure of the Human Rad9-Rad1-Hus1 DNA Damage Checkpoint Complex===
		+	{{ABSTRACT_PUBMED_19446481}}

-	~~{{ABSTRACT_PUBMED_19446481}}~~	+	==Function==
		+	[[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/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> [[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>

	==About this Structure==		==About this Structure==
Line 11:		Line 10:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:019446481</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019446481</ref><references group="xtra"/><references/>
	[[Category: Exodeoxyribonuclease III]]		[[Category: Exodeoxyribonuclease III]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA: Protected "3g65" [edit=sysop:move=sysop]

OCA — Wed, 20 Feb 2013 14:44:55 GMT

Protected "3g65" [edit=sysop:move=sysop]

←Older revision

Revision as of 14:44, 20 February 2013

OCA at 14:44, 20 February 2013

OCA — Wed, 20 Feb 2013 14:44:50 GMT

←Older revision		Revision as of 14:44, 20 February 2013
Line 1:		Line 1:
-	~~{{Seed}}~~	+	[[Image:3g65.png\|left\|200px]]
-	[[Image:3g65.~~jpg~~\|left\|200px]]	+

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3g65", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_3g65\| PDB=3g65 \| SCENE= }}		{{STRUCTURE_3g65\| PDB=3g65 \| SCENE= }}

	===Crystal Structure of the Human Rad9-Rad1-Hus1 DNA Damage Checkpoint Complex===		===Crystal Structure of the Human Rad9-Rad1-Hus1 DNA Damage Checkpoint Complex===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_19446481}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 19446481 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_19446481}}		{{ABSTRACT_PUBMED_19446481}}

	==About this Structure==		==About this Structure==
-	~~3G65~~ is a 3 ~~chains~~ structure ~~of sequences~~ 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=3G65 OCA].	+	[[3g65]] is a 3 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=3G65 OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~19446481~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019446481</ref><references group="xtra"/>
	[[Category: Exodeoxyribonuclease III]]		[[Category: Exodeoxyribonuclease III]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
Line 30:		Line 18:
	[[Category: Pearl, L H.]]		[[Category: Pearl, L H.]]
	[[Category: Rzechorzek, N J.]]		[[Category: Rzechorzek, N J.]]
-	[[Category: Alternative splicing]]
	[[Category: Cell cycle]]		[[Category: Cell cycle]]
-	[[Category: Cytoplasm]]
	[[Category: Dna binding clamp]]		[[Category: Dna binding clamp]]
	[[Category: Dna damage]]		[[Category: Dna damage]]
Line 42:		Line 28:
	[[Category: Pcna]]		[[Category: Pcna]]
	[[Category: Phosphoprotein]]		[[Category: Phosphoprotein]]
-	[[Category: Polymorphism]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 27 15:21:24 2009''

OCA at 12:21, 27 May 2009

OCA — Wed, 27 May 2009 12:21:24 GMT

←Older revision		Revision as of 12:21, 27 May 2009
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{Seed}}
		+	[[Image:3g65.jpg\|left\|200px]]

-	The ~~entry 3g65~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3g65", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3g65\| PDB=3g65 \| SCENE= }}

-	~~Authors: Dore, A.S., Kilkenny, M.L., Rzechorzek, N.J., Pearl, L.H.~~	+	===Crystal Structure of the Human Rad9-Rad1-Hus1 DNA Damage Checkpoint Complex===

-	Description: Crystal Structure of the Human Rad9-Rad1-Hus1 DNA Damage Checkpoint Complex

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Feb 25 09~~:26:55 2009''	+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_19446481}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 19446481 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_19446481}}
		+
		+	==About this Structure==
		+	3G65 is a 3 chains structure of sequences 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=3G65 OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:19446481</ref><references group="xtra"/>
		+	[[Category: Exodeoxyribonuclease III]]
		+	[[Category: Homo sapiens]]
		+	[[Category: Dore, A S.]]
		+	[[Category: Kilkenny, M L.]]
		+	[[Category: Pearl, L H.]]
		+	[[Category: Rzechorzek, N J.]]
		+	[[Category: Alternative splicing]]
		+	[[Category: Cell cycle]]
		+	[[Category: Cytoplasm]]
		+	[[Category: Dna binding clamp]]
		+	[[Category: Dna damage]]
		+	[[Category: Dna repair]]
		+	[[Category: Exonuclease]]
		+	[[Category: Hydrolase]]
		+	[[Category: Nuclease]]
		+	[[Category: Nucleus]]
		+	[[Category: Pcna]]
		+	[[Category: Phosphoprotein]]
		+	[[Category: Polymorphism]]
		+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 27 15:21:24 2009''