3aaf - Revision history

OCA at 14:00, 13 March 2024

2024-03-13T14:00:16Z

←Older revision		Revision as of 14:00, 13 March 2024
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	<StructureSection load='3aaf' size='340' side='right'caption='[[3aaf]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='3aaf' size='340' side='right'caption='[[3aaf]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3aaf]] is a 4 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=3AAF OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=3AAF FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3aaf]] is a 4 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=3AAF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AAF FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></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]] 1.9Å</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=3aaf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aaf OCA], [~~http~~://pdbe.org/3aaf PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3aaf RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3aaf PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3aaf ProSAT]</span></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></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=3aaf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aaf OCA], [https://pdbe.org/3aaf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aaf RCSB], [https://www.ebi.ac.uk/pdbsum/3aaf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aaf ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/WRN_HUMAN WRN_HUMAN]] Defects in WRN are a cause of Werner syndrome (WRN) [MIM:[~~http~~://omim.org/entry/277700 277700]]. WRN is a rare autosomal recessive progeroid syndrome characterized by the premature onset of multiple age-related disorders, including atherosclerosis, cancer, non-insulin-dependent diabetes mellitus, ocular cataracts and osteoporosis. The major cause of death, at a median age of 47, is myocardial infarction. Currently all known WS mutations produces prematurely terminated proteins.<ref>PMID:16673358</ref> Defects in WRN may be a cause of colorectal cancer (CRC) [MIM:[~~http~~://omim.org/entry/114500 114500]].	+	[https://www.uniprot.org/uniprot/WRN_HUMAN WRN_HUMAN] Defects in WRN are a cause of Werner syndrome (WRN) [MIM:[https://omim.org/entry/277700 277700]. WRN is a rare autosomal recessive progeroid syndrome characterized by the premature onset of multiple age-related disorders, including atherosclerosis, cancer, non-insulin-dependent diabetes mellitus, ocular cataracts and osteoporosis. The major cause of death, at a median age of 47, is myocardial infarction. Currently all known WS mutations produces prematurely terminated proteins.<ref>PMID:16673358</ref> Defects in WRN may be a cause of colorectal cancer (CRC) [MIM:[https://omim.org/entry/114500 114500].
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/WRN_HUMAN WRN_HUMAN]] Multifunctional enzyme that has both magnesium and ATP-dependent DNA-helicase activity and 3'->5' exonuclease activity towards double-stranded DNA with a 5'-overhang. Has no nuclease activity towards single-stranded DNA or blunt-ended double-stranded DNA. Binds preferentially to DNA substrates containing alternate secondary structures, such as replication forks and Holliday junctions. May play an important role in the dissociation of joint DNA molecules that can arise as products of homologous recombination, at stalled replication forks or during DNA repair. Alleviates stalling of DNA polymerases at the site of DNA lesions. Important for genomic integrity. Plays a role in the formation of DNA replication focal centers; stably associates with foci elements generating binding sites for RP-A (By similarity).<ref>PMID:11863428</ref> <ref>PMID:17563354</ref> <ref>PMID:18596042</ref> <ref>PMID:19652551</ref> <ref>PMID:19283071</ref>	+	[https://www.uniprot.org/uniprot/WRN_HUMAN WRN_HUMAN] Multifunctional enzyme that has both magnesium and ATP-dependent DNA-helicase activity and 3'->5' exonuclease activity towards double-stranded DNA with a 5'-overhang. Has no nuclease activity towards single-stranded DNA or blunt-ended double-stranded DNA. Binds preferentially to DNA substrates containing alternate secondary structures, such as replication forks and Holliday junctions. May play an important role in the dissociation of joint DNA molecules that can arise as products of homologous recombination, at stalled replication forks or during DNA repair. Alleviates stalling of DNA polymerases at the site of DNA lesions. Important for genomic integrity. Plays a role in the formation of DNA replication focal centers; stably associates with foci elements generating binding sites for RP-A (By similarity).<ref>PMID:11863428</ref> <ref>PMID:17563354</ref> <ref>PMID:18596042</ref> <ref>PMID:19652551</ref> <ref>PMID:19283071</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</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=3aaf 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=3aaf ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The RecQ family of DNA helicases including WRN (Werner syndrome protein) and BLM (Bloom syndrome protein) protects the genome against deleterious changes. Here we report the cocrystal structure of the RecQ C-terminal (RQC) domain of human WRN bound to a DNA duplex. In the complex, the RQC domain specifically interacted with a blunt end of the duplex and, surprisingly, unpaired a Watson-Crick base pair in the absence of an ATPase domain. The beta wing, an extended hairpin motif that is characteristic of winged-helix motifs, was used as a "separating knife" to wedge between the first and second base pairs, whereas the recognition helix, a principal component of helix-turn-helix motifs that are usually embedded within DNA grooves, was unprecedentedly excluded from the interaction. Our results demonstrate a function of the winged-helix motif central to the helicase reaction, establishing the first structural paradigm concerning the DNA structure-specific activities of the RecQ helicases.
-
-	Structural basis for DNA strand separation by the unconventional winged-helix domain of RecQ helicase WRN.,Kitano K, Kim SY, Hakoshima T Structure. 2010 Feb 10;18(2):177-87. PMID:20159463<ref>PMID:20159463</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 3aaf" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Hakoshima, T]]	+	[[Category: Hakoshima T]]
-	[[Category: Kitano, K]]	+	[[Category: Kitano K]]
-	~~[[Category: Dna binding protein-dna complex]]~~	+
-	~~[[Category: Dna-binding]]~~	+
-	~~[[Category: Helicase]]~~	+
-	~~[[Category: Helix-turn-helix]]~~	+
-	~~[[Category: Protein-dna complex]]~~	+
-	~~[[Category: Winged-helix~~]]	+

OCA at 12:20, 29 July 2020

2020-07-29T12:20:28Z

←Older revision		Revision as of 12:20, 29 July 2020
Line 1:		Line 1:

	==Structure of WRN RQC domain bound to double-stranded DNA==		==Structure of WRN RQC domain bound to double-stranded DNA==
-	<StructureSection load='3aaf' size='340' side='right' caption='[[3aaf]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='3aaf' size='340' side='right'caption='[[3aaf]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3aaf]] is a 4 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=3AAF OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3AAF FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3aaf]] is a 4 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=3AAF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3AAF FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></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=3aaf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aaf OCA], [http://pdbe.org/3aaf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3aaf RCSB], [http://www.ebi.ac.uk/pdbsum/3aaf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3aaf ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3aaf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aaf OCA], [http://pdbe.org/3aaf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3aaf RCSB], [http://www.ebi.ac.uk/pdbsum/3aaf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3aaf ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 32:		Line 32:

	==See Also==		==See Also==
-	*[[Helicase\|Helicase]]	+	*[[Helicase 3D structures\|Helicase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 38:		Line 38:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Hakoshima, T]]		[[Category: Hakoshima, T]]
	[[Category: Kitano, K]]		[[Category: Kitano, K]]

OCA at 08:14, 24 October 2018

2018-10-24T08:14:14Z

←Older revision		Revision as of 08:14, 24 October 2018
Line 15:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aa/3aaf_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aa/3aaf_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 14:02, 11 August 2016

2016-08-11T14:02:16Z

←Older revision		Revision as of 14:02, 11 August 2016
Line 1:		Line 1:
		+
	==Structure of WRN RQC domain bound to double-stranded DNA==		==Structure of WRN RQC domain bound to double-stranded DNA==
	<StructureSection load='3aaf' size='340' side='right' caption='[[3aaf]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='3aaf' size='340' side='right' caption='[[3aaf]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3aaf]] is a 4 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=3AAF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AAF FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3aaf]] is a 4 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=3AAF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AAF FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></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=3aaf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aaf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3aaf RCSB], [http://www.ebi.ac.uk/pdbsum/3aaf 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=3aaf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aaf OCA], [http://pdbe.org/3aaf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3aaf RCSB], [http://www.ebi.ac.uk/pdbsum/3aaf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3aaf ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	<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=3aaf ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 28:		Line 29:
	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 3aaf" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 37:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Hakoshima, T]]		[[Category: Hakoshima, T]]
	[[Category: Kitano, K]]		[[Category: Kitano, K]]

OCA at 11:49, 20 January 2015

2015-01-20T11:49:45Z

←Older revision		Revision as of 11:49, 20 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3aaf]] is a 4 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=3AAF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AAF FirstGlance]. <br>		<table><tr><td colspan='2'>[[3aaf]] is a 4 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=3AAF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AAF FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3aaf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aaf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3aaf RCSB], [http://www.ebi.ac.uk/pdbsum/3aaf 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=3aaf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aaf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3aaf RCSB], [http://www.ebi.ac.uk/pdbsum/3aaf PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/WRN_HUMAN WRN_HUMAN]] Defects in WRN are a cause of Werner syndrome (WRN) [MIM:[http://omim.org/entry/277700 277700]]. WRN is a rare autosomal recessive progeroid syndrome characterized by the premature onset of multiple age-related disorders, including atherosclerosis, cancer, non-insulin-dependent diabetes mellitus, ocular cataracts and osteoporosis. The major cause of death, at a median age of 47, is myocardial infarction. Currently all known WS mutations produces prematurely terminated proteins.<ref>PMID:16673358</ref> Defects in WRN may be a cause of colorectal cancer (CRC) [MIM:[http://omim.org/entry/114500 114500]].		[[http://www.uniprot.org/uniprot/WRN_HUMAN WRN_HUMAN]] Defects in WRN are a cause of Werner syndrome (WRN) [MIM:[http://omim.org/entry/277700 277700]]. WRN is a rare autosomal recessive progeroid syndrome characterized by the premature onset of multiple age-related disorders, including atherosclerosis, cancer, non-insulin-dependent diabetes mellitus, ocular cataracts and osteoporosis. The major cause of death, at a median age of 47, is myocardial infarction. Currently all known WS mutations produces prematurely terminated proteins.<ref>PMID:16673358</ref> Defects in WRN may be a cause of colorectal cancer (CRC) [MIM:[http://omim.org/entry/114500 114500]].
Line 36:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Hakoshima, T.]]	+	[[Category: Hakoshima, T]]
-	[[Category: Kitano, K.]]	+	[[Category: Kitano, K]]
	[[Category: Dna binding protein-dna complex]]		[[Category: Dna binding protein-dna complex]]
	[[Category: Dna-binding]]		[[Category: Dna-binding]]

OCA at 05:39, 2 October 2014

2014-10-02T05:39:38Z

←Older revision		Revision as of 05:39, 2 October 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3aaf~~\| ~~PDB~~=3aaf \| ~~SCENE~~= }}	+	==Structure of WRN RQC domain bound to double-stranded DNA==
-	===~~Structure~~ of WRN ~~RQC domain bound to~~ double-stranded DNA===	+	<StructureSection load='3aaf' size='340' side='right' caption='[[3aaf]], [[Resolution\|resolution]] 1.90Å' scene=''>
-	~~{{ABSTRACT_PUBMED_20159463}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3aaf]] is a 4 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=3AAF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AAF FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene><br>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3aaf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aaf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3aaf RCSB], [http://www.ebi.ac.uk/pdbsum/3aaf PDBsum]</span></td></tr>
		+	<table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/WRN_HUMAN WRN_HUMAN]] Defects in WRN are a cause of Werner syndrome (WRN) [MIM:[http://omim.org/entry/277700 277700]]. WRN is a rare autosomal recessive progeroid syndrome characterized by the premature onset of multiple age-related disorders, including atherosclerosis, cancer, non-insulin-dependent diabetes mellitus, ocular cataracts and osteoporosis. The major cause of death, at a median age of 47, is myocardial infarction. Currently all known WS mutations produces prematurely terminated proteins.<ref>PMID:16673358</ref> Defects in WRN may be a cause of colorectal cancer (CRC) [MIM:[http://omim.org/entry/114500 114500]].
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/WRN_HUMAN WRN_HUMAN]] Multifunctional enzyme that has both magnesium and ATP-dependent DNA-helicase activity and 3'->5' exonuclease activity towards double-stranded DNA with a 5'-overhang. Has no nuclease activity towards single-stranded DNA or blunt-ended double-stranded DNA. Binds preferentially to DNA substrates containing alternate secondary structures, such as replication forks and Holliday junctions. May play an important role in the dissociation of joint DNA molecules that can arise as products of homologous recombination, at stalled replication forks or during DNA repair. Alleviates stalling of DNA polymerases at the site of DNA lesions. Important for genomic integrity. Plays a role in the formation of DNA replication focal centers; stably associates with foci elements generating binding sites for RP-A (By similarity).<ref>PMID:11863428</ref> <ref>PMID:17563354</ref> <ref>PMID:18596042</ref> <ref>PMID:19652551</ref> <ref>PMID:19283071</ref>
		+	== 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/aa/3aaf_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 ==
		+	The RecQ family of DNA helicases including WRN (Werner syndrome protein) and BLM (Bloom syndrome protein) protects the genome against deleterious changes. Here we report the cocrystal structure of the RecQ C-terminal (RQC) domain of human WRN bound to a DNA duplex. In the complex, the RQC domain specifically interacted with a blunt end of the duplex and, surprisingly, unpaired a Watson-Crick base pair in the absence of an ATPase domain. The beta wing, an extended hairpin motif that is characteristic of winged-helix motifs, was used as a "separating knife" to wedge between the first and second base pairs, whereas the recognition helix, a principal component of helix-turn-helix motifs that are usually embedded within DNA grooves, was unprecedentedly excluded from the interaction. Our results demonstrate a function of the winged-helix motif central to the helicase reaction, establishing the first structural paradigm concerning the DNA structure-specific activities of the RecQ helicases.

-	~~==Disease==~~	+	Structural basis for DNA strand separation by the unconventional winged-helix domain of RecQ helicase WRN.,Kitano K, Kim SY, Hakoshima T Structure. 2010 Feb 10;18(2):177-87. PMID:20159463<ref>PMID:20159463</ref>
-	~~[[http://www.uniprot.org/uniprot/WRN_HUMAN WRN_HUMAN]] Defects in WRN are a cause~~ of ~~Werner syndrome (~~WRN~~) [MIM:[http://omim~~.~~org/entry/277700 277700]]. WRN is a rare autosomal recessive progeroid syndrome characterized by the premature onset of multiple age-related disorders~~, ~~including atherosclerosis~~, ~~cancer~~, ~~non~~-insulin-dependent diabetes mellitus, ocular cataracts and osteoporosis. The major cause of death, at a median age of 47, is myocardial infarction. Currently all known WS mutations produces prematurely terminated proteins.<ref>PMID:~~16673358~~</ref> ~~Defects in WRN may be a cause of colorectal cancer (CRC) [MIM:[http://omim.org/entry/114500 114500]].~~	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www.uniprot.org/uniprot/WRN_HUMAN WRN_HUMAN]] Multifunctional enzyme that has both magnesium and ATP-dependent DNA-helicase activity and 3'->5' exonuclease activity towards double-stranded DNA with~~ a 5'-overhang. Has no nuclease activity towards single-stranded DNA or blunt-ended double-stranded DNA. Binds preferentially to DNA substrates containing alternate secondary structures, such as replication forks and Holliday junctions. May play an important role in the dissociation of joint DNA molecules that can arise as products of homologous recombination, at stalled replication forks or during DNA repair. Alleviates stalling of ~~DNA polymerases at~~ the ~~site of DNA lesions~~. ~~Important for genomic integrity~~. ~~Plays a role in the formation~~ of ~~DNA replication focal centers; stably associates with foci elements generating binding sites for RP-A (By similarity)~~.<~~ref~~>~~PMID:11863428~~</~~ref~~>~~<ref>PMID:17563354</ref><ref>PMID:18596042</ref><ref>PMID:19652551</ref><ref>PMID:19283071</ref>~~	+	</div>
-		+
-	~~==About this Structure==~~	+
-	[[3aaf]] is a 4 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=3AAF OCA].	+

	==See Also==		==See Also==
	*[[Helicase\|Helicase]]		*[[Helicase\|Helicase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:020159463</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Hakoshima, T.]]		[[Category: Hakoshima, T.]]

OCA at 22:33, 24 March 2013

2013-03-24T22:33:47Z

←Older revision		Revision as of 22:33, 24 March 2013
Line 1:		Line 1:
-	[[Image:3aaf.png\|left\|200px]]
-
	{{STRUCTURE_3aaf\| PDB=3aaf \| SCENE= }}		{{STRUCTURE_3aaf\| PDB=3aaf \| SCENE= }}
-
	===Structure of WRN RQC domain bound to double-stranded DNA===		===Structure of WRN RQC domain bound to double-stranded DNA===
		+	{{ABSTRACT_PUBMED_20159463}}

-	~~{{ABSTRACT_PUBMED_20159463}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/WRN_HUMAN WRN_HUMAN]] Defects in WRN are a cause of Werner syndrome (WRN) [MIM:[http://omim.org/entry/277700 277700]]. WRN is a rare autosomal recessive progeroid syndrome characterized by the premature onset of multiple age-related disorders, including atherosclerosis, cancer, non-insulin-dependent diabetes mellitus, ocular cataracts and osteoporosis. The major cause of death, at a median age of 47, is myocardial infarction. Currently all known WS mutations produces prematurely terminated proteins.<ref>PMID:16673358</ref> Defects in WRN may be a cause of colorectal cancer (CRC) [MIM:[http://omim.org/entry/114500 114500]].
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/WRN_HUMAN WRN_HUMAN]] Multifunctional enzyme that has both magnesium and ATP-dependent DNA-helicase activity and 3'->5' exonuclease activity towards double-stranded DNA with a 5'-overhang. Has no nuclease activity towards single-stranded DNA or blunt-ended double-stranded DNA. Binds preferentially to DNA substrates containing alternate secondary structures, such as replication forks and Holliday junctions. May play an important role in the dissociation of joint DNA molecules that can arise as products of homologous recombination, at stalled replication forks or during DNA repair. Alleviates stalling of DNA polymerases at the site of DNA lesions. Important for genomic integrity. Plays a role in the formation of DNA replication focal centers; stably associates with foci elements generating binding sites for RP-A (By similarity).<ref>PMID:11863428</ref><ref>PMID:17563354</ref><ref>PMID:18596042</ref><ref>PMID:19652551</ref><ref>PMID:19283071</ref>

	==About this Structure==		==About this Structure==
Line 14:		Line 16:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:020159463</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020159463</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Hakoshima, T.]]		[[Category: Hakoshima, T.]]

OCA at 20:15, 20 October 2012

2012-10-20T20:15:59Z

←Older revision		Revision as of 20:15, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3aaf]] is a 4 chain structure ~~of [[Helicase]]~~ 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=3AAF OCA].	+	[[3aaf]] is a 4 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=3AAF OCA].

	==See Also==		==See Also==

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

2012-07-27T09:55:54Z

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

←Older revision

Revision as of 09:55, 27 July 2012

OCA at 09:55, 27 July 2012

2012-07-27T09:55:52Z

←Older revision		Revision as of 09:55, 27 July 2012
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-	{{Seed}}
	[[Image:3aaf.png\|left\|200px]]		[[Image:3aaf.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3aaf", 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_3aaf\| PDB=3aaf \| SCENE= }}		{{STRUCTURE_3aaf\| PDB=3aaf \| SCENE= }}

	===Structure of WRN RQC domain bound to double-stranded DNA===		===Structure of WRN RQC domain bound to double-stranded DNA===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_20159463}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 20159463 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_20159463}}		{{ABSTRACT_PUBMED_20159463}}

	==About this Structure==		==About this Structure==
-	~~3AAF~~ is a 4 ~~chains~~ structure with ~~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=3AAF OCA].	+	[[3aaf]] is a 4 chain structure of [[Helicase]] 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=3AAF OCA].
		+
		+	==See Also==
		+	*[[Helicase\|Helicase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~20159463~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020159463</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Hakoshima, T.]]		[[Category: Hakoshima, T.]]
Line 33:		Line 24:
	[[Category: Protein-dna complex]]		[[Category: Protein-dna complex]]
	[[Category: Winged-helix]]		[[Category: Winged-helix]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 14 08:59:05 2010''