1w0u - Revision history

OCA at 09:09, 9 May 2024

OCA — Thu, 09 May 2024 09:09:00 GMT

←Older revision		Revision as of 09:09, 9 May 2024
Line 3:		Line 3:
	<StructureSection load='1w0u' size='340' side='right'caption='[[1w0u]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='1w0u' size='340' side='right'caption='[[1w0u]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1w0u]] is a 4 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=1W0U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W0U FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1w0u]] 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=1W0U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W0U FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat">~~<div style='overflow: auto; max~~-~~height: 3em;'>~~[[~~1h6p~~\|~~1h6p~~]]~~</div>~~</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]] 1.8Å</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=1w0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w0u OCA], [https://pdbe.org/1w0u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w0u RCSB], [https://www.ebi.ac.uk/pdbsum/1w0u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w0u 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=1w0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w0u OCA], [https://pdbe.org/1w0u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w0u RCSB], [https://www.ebi.ac.uk/pdbsum/1w0u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w0u ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/TERF2_HUMAN TERF2_HUMAN]] Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and plays a central role in telomere maintenance and protection against end-to-end fusion of chromosomes. In addition to its telomeric DNA-binding role, required to recruit a number of factors and enzymes required for telomere protection, including the shelterin complex, TERF2IP/RAP1 and DCLRE1B/Apollo. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Together with DCLRE1B/Apollo, plays a key role in telomeric loop (T loop) formation by generating 3' single-stranded overhang at the leading end telomeres: T loops have been proposed to protect chromosome ends from degradation and repair. Required both to recruit DCLRE1B/Apollo to telomeres and activate the exonuclease activity of DCLRE1B/Apollo. Preferentially binds to positive supercoiled DNA. Together with DCLRE1B/Apollo, required to control the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology. Recruits TERF2IP/RAP1 to telomeres, thereby participating in to repressing homology-directed repair (HDR), which can affect telomere length.<ref>PMID:9476899</ref> <ref>PMID:16166375</ref> <ref>PMID:20655466</ref>	+	[https://www.uniprot.org/uniprot/TERF2_HUMAN TERF2_HUMAN] Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and plays a central role in telomere maintenance and protection against end-to-end fusion of chromosomes. In addition to its telomeric DNA-binding role, required to recruit a number of factors and enzymes required for telomere protection, including the shelterin complex, TERF2IP/RAP1 and DCLRE1B/Apollo. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Together with DCLRE1B/Apollo, plays a key role in telomeric loop (T loop) formation by generating 3' single-stranded overhang at the leading end telomeres: T loops have been proposed to protect chromosome ends from degradation and repair. Required both to recruit DCLRE1B/Apollo to telomeres and activate the exonuclease activity of DCLRE1B/Apollo. Preferentially binds to positive supercoiled DNA. Together with DCLRE1B/Apollo, required to control the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology. Recruits TERF2IP/RAP1 to telomeres, thereby participating in to repressing homology-directed repair (HDR), which can affect telomere length.<ref>PMID:9476899</ref> <ref>PMID:16166375</ref> <ref>PMID:20655466</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 32:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Chapman~~, L M~~]]	+	[[Category: Chapman LM]]
-	[[Category: Court~~, R I~~]]	+	[[Category: Court RI]]
-	[[Category: Fairall, L]]	+	[[Category: Fairall L]]
-	[[Category: Rhodes, D]]	+	[[Category: Rhodes D]]
-	~~[[Category: Adp-ribosylation]]~~	+
-	~~[[Category: Cell cycle]]~~	+
-	~~[[Category: Chromosomal protein]]~~	+
-	~~[[Category: Dna binding protein]]~~	+
-	~~[[Category: Dna-binding protein]]~~	+
-	~~[[Category: Homeodomain]]~~	+
-	~~[[Category: Mitosis]]~~	+
-	~~[[Category: Nuclear protein]]~~	+
-	~~[[Category: Phosphorylation]]~~	+
-	~~[[Category: Telomere~~]]	+

OCA at 13:29, 13 October 2021

OCA — Wed, 13 Oct 2021 13:29:42 GMT

←Older revision		Revision as of 13:29, 13 October 2021
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	<StructureSection load='1w0u' size='340' side='right'caption='[[1w0u]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='1w0u' size='340' side='right'caption='[[1w0u]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1w0u]] 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=1W0U OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1W0U FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1w0u]] is a 4 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=1W0U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W0U FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1h6p\|1h6p]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1h6p\|1h6p]]</div></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=1w0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w0u OCA], [~~http~~://pdbe.org/1w0u PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1w0u RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1w0u PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1w0u 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=1w0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w0u OCA], [https://pdbe.org/1w0u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w0u RCSB], [https://www.ebi.ac.uk/pdbsum/1w0u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w0u ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/TERF2_HUMAN TERF2_HUMAN]] Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and plays a central role in telomere maintenance and protection against end-to-end fusion of chromosomes. In addition to its telomeric DNA-binding role, required to recruit a number of factors and enzymes required for telomere protection, including the shelterin complex, TERF2IP/RAP1 and DCLRE1B/Apollo. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Together with DCLRE1B/Apollo, plays a key role in telomeric loop (T loop) formation by generating 3' single-stranded overhang at the leading end telomeres: T loops have been proposed to protect chromosome ends from degradation and repair. Required both to recruit DCLRE1B/Apollo to telomeres and activate the exonuclease activity of DCLRE1B/Apollo. Preferentially binds to positive supercoiled DNA. Together with DCLRE1B/Apollo, required to control the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology. Recruits TERF2IP/RAP1 to telomeres, thereby participating in to repressing homology-directed repair (HDR), which can affect telomere length.<ref>PMID:9476899</ref> <ref>PMID:16166375</ref> <ref>PMID:20655466</ref>	+	[[https://www.uniprot.org/uniprot/TERF2_HUMAN TERF2_HUMAN]] Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and plays a central role in telomere maintenance and protection against end-to-end fusion of chromosomes. In addition to its telomeric DNA-binding role, required to recruit a number of factors and enzymes required for telomere protection, including the shelterin complex, TERF2IP/RAP1 and DCLRE1B/Apollo. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Together with DCLRE1B/Apollo, plays a key role in telomeric loop (T loop) formation by generating 3' single-stranded overhang at the leading end telomeres: T loops have been proposed to protect chromosome ends from degradation and repair. Required both to recruit DCLRE1B/Apollo to telomeres and activate the exonuclease activity of DCLRE1B/Apollo. Preferentially binds to positive supercoiled DNA. Together with DCLRE1B/Apollo, required to control the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology. Recruits TERF2IP/RAP1 to telomeres, thereby participating in to repressing homology-directed repair (HDR), which can affect telomere length.<ref>PMID:9476899</ref> <ref>PMID:16166375</ref> <ref>PMID:20655466</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 10:24, 8 January 2020

OCA — Wed, 08 Jan 2020 10:24:57 GMT

←Older revision		Revision as of 10:24, 8 January 2020
Line 1:		Line 1:

	==hTRF2 DNA-binding domain in complex with telomeric DNA.==		==hTRF2 DNA-binding domain in complex with telomeric DNA.==
-	<StructureSection load='1w0u' size='340' side='right' caption='[[1w0u]], [[Resolution\|resolution]] 1.80Å' scene=''>	+	<StructureSection load='1w0u' size='340' side='right'caption='[[1w0u]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1w0u]] 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=1W0U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W0U FirstGlance]. <br>		<table><tr><td colspan='2'>[[1w0u]] 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=1W0U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W0U FirstGlance]. <br>
Line 33:		Line 33:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Chapman, L M]]		[[Category: Chapman, L M]]
	[[Category: Court, R I]]		[[Category: Court, R I]]

OCA at 07:30, 4 April 2018

OCA — Wed, 04 Apr 2018 07:30:10 GMT

←Older revision		Revision as of 07:30, 4 April 2018
Line 1:		Line 1:
-	==~~HTRF2~~ DNA-~~BINDING DOMAIN IN COMPLEX WITH TELOMERIC~~ DNA.==	+
		+	==hTRF2 DNA-binding domain in complex with telomeric DNA.==
	<StructureSection load='1w0u' size='340' side='right' caption='[[1w0u]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='1w0u' size='340' side='right' caption='[[1w0u]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1w0u]] 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=1W0U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W0U FirstGlance]. <br>		<table><tr><td colspan='2'>[[1w0u]] 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=1W0U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W0U FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1h6p\|1h6p]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1h6p\|1h6p]]</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=1w0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w0u OCA], [http://pdbe.org/1w0u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1w0u RCSB], [http://www.ebi.ac.uk/pdbsum/1w0u 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=1w0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w0u OCA], [http://pdbe.org/1w0u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1w0u RCSB], [http://www.ebi.ac.uk/pdbsum/1w0u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1w0u ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 12:		Line 13:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w0/1w0u_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w0/1w0u_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>
Line 39:		Line 40:
	[[Category: Cell cycle]]		[[Category: Cell cycle]]
	[[Category: Chromosomal protein]]		[[Category: Chromosomal protein]]
		+	[[Category: Dna binding protein]]
	[[Category: Dna-binding protein]]		[[Category: Dna-binding protein]]
	[[Category: Homeodomain]]		[[Category: Homeodomain]]

OCA at 11:29, 8 February 2016

OCA — Mon, 08 Feb 2016 11:29:38 GMT

←Older revision		Revision as of 11:29, 8 February 2016
Line 16:		Line 16:
	<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=1w0u ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 11:07, 10 September 2015

OCA — Thu, 10 Sep 2015 11:07:04 GMT

←Older revision		Revision as of 11:07, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1w0u' size='340' side='right' caption='[[1w0u]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='1w0u' size='340' side='right' caption='[[1w0u]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1w0u]] 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=1W0U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W0U FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1w0u]] 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=1W0U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W0U FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1h6p\|1h6p]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1h6p\|1h6p]]</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=1w0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w0u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1w0u RCSB], [http://www.ebi.ac.uk/pdbsum/1w0u 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=1w0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w0u OCA], [http://pdbe.org/1w0u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1w0u RCSB], [http://www.ebi.ac.uk/pdbsum/1w0u PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/TERF2_HUMAN TERF2_HUMAN]] Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and plays a central role in telomere maintenance and protection against end-to-end fusion of chromosomes. In addition to its telomeric DNA-binding role, required to recruit a number of factors and enzymes required for telomere protection, including the shelterin complex, TERF2IP/RAP1 and DCLRE1B/Apollo. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Together with DCLRE1B/Apollo, plays a key role in telomeric loop (T loop) formation by generating 3' single-stranded overhang at the leading end telomeres: T loops have been proposed to protect chromosome ends from degradation and repair. Required both to recruit DCLRE1B/Apollo to telomeres and activate the exonuclease activity of DCLRE1B/Apollo. Preferentially binds to positive supercoiled DNA. Together with DCLRE1B/Apollo, required to control the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology. Recruits TERF2IP/RAP1 to telomeres, thereby participating in to repressing homology-directed repair (HDR), which can affect telomere length.<ref>PMID:9476899</ref> <ref>PMID:16166375</ref> <ref>PMID:20655466</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 24:		Line 26:
	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 1w0u" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Chapman, L M]]		[[Category: Chapman, L M]]
	[[Category: Court, R I]]		[[Category: Court, R I]]

OCA at 13:40, 6 January 2015

OCA — Tue, 06 Jan 2015 13:40:22 GMT

←Older revision		Revision as of 13:40, 6 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1w0u]] 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=1W0U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W0U FirstGlance]. <br>		<table><tr><td colspan='2'>[[1w0u]] 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=1W0U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W0U FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1h6p\|1h6p]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1h6p\|1h6p]]</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=1w0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w0u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1w0u RCSB], [http://www.ebi.ac.uk/pdbsum/1w0u 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=1w0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w0u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1w0u RCSB], [http://www.ebi.ac.uk/pdbsum/1w0u PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 29:		Line 29:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Chapman, L M.]]	+	[[Category: Chapman, L M]]
-	[[Category: Court, R I.]]	+	[[Category: Court, R I]]
-	[[Category: Fairall, L.]]	+	[[Category: Fairall, L]]
-	[[Category: Rhodes, D.]]	+	[[Category: Rhodes, D]]
	[[Category: Adp-ribosylation]]		[[Category: Adp-ribosylation]]
	[[Category: Cell cycle]]		[[Category: Cell cycle]]

OCA at 19:04, 29 September 2014

OCA — Mon, 29 Sep 2014 19:04:33 GMT

←Older revision		Revision as of 19:04, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1w0u.~~png~~\|~~left~~\|200px]]	+	==HTRF2 DNA-BINDING DOMAIN IN COMPLEX WITH TELOMERIC DNA.==
		+	<StructureSection load='1w0u' size='340' side='right' caption='[[1w0u]], [[Resolution\|resolution]] 1.80Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1w0u]] 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=1W0U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W0U FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1h6p\|1h6p]]</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=1w0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w0u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1w0u RCSB], [http://www.ebi.ac.uk/pdbsum/1w0u 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/w0/1w0u_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 ==
		+	Human telomeres consist of tandem arrays of TTAGGG sequence repeats that are specifically bound by two proteins, TRF1 and TRF2. They bind to DNA as preformed homodimers and have the same architecture in which the DNA-binding domains (Dbds) form independent structural units. Despite these similarities, TRF1 and TRF2 have different functions at telomeres. The X-ray crystal structures of both TRF1- and TRF2-Dbds in complex with telomeric DNA (2.0 and 1.8 angstroms resolution, respectively) show that they recognize the same TAGGGTT binding site by means of homeodomains, as does the yeast telomeric protein Rap1p. Two of the three G-C base pairs that characterize telomeric repeats are recognized specifically and an unusually large number of water molecules mediate protein-DNA interactions. The binding of the TRF2-Dbd to the DNA double helix shows no distortions that would account for the promotion of t-loops in which TRF2 has been implicated.

-	~~{{STRUCTURE_1w0u\| PDB=1w0u \| SCENE= }}~~	+	How the human telomeric proteins TRF1 and TRF2 recognize telomeric DNA: a view from high-resolution crystal structures.,Court R, Chapman L, Fairall L, Rhodes D EMBO Rep. 2005 Jan;6(1):39-45. PMID:15608617<ref>PMID:15608617</ref>

-	~~===HTRF2 DNA-BINDING DOMAIN IN COMPLEX WITH TELOMERIC DNA.===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_15608617}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1w0u]] 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=1W0U OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:015608617<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Chapman, L M.]]		[[Category: Chapman, L M.]]

OCA at 12:38, 23 January 2013

OCA — Wed, 23 Jan 2013 12:38:28 GMT

←Older revision		Revision as of 12:38, 23 January 2013
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	[[Image:1w0u.png\|left\|200px]]		[[Image:1w0u.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1w0u", 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_1w0u\| PDB=1w0u \| SCENE= }}		{{STRUCTURE_1w0u\| PDB=1w0u \| SCENE= }}

	===HTRF2 DNA-BINDING DOMAIN IN COMPLEX WITH TELOMERIC DNA.===		===HTRF2 DNA-BINDING DOMAIN IN COMPLEX WITH TELOMERIC DNA.===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_15608617}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 15608617 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_15608617}}		{{ABSTRACT_PUBMED_15608617}}

Line 22:		Line 11:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~15608617~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:015608617</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Chapman, L M.]]		[[Category: Chapman, L M.]]
Line 28:		Line 17:
	[[Category: Fairall, L.]]		[[Category: Fairall, L.]]
	[[Category: Rhodes, D.]]		[[Category: Rhodes, D.]]
		+	[[Category: Adp-ribosylation]]
		+	[[Category: Cell cycle]]
		+	[[Category: Chromosomal protein]]
		+	[[Category: Dna-binding protein]]
		+	[[Category: Homeodomain]]
		+	[[Category: Mitosis]]
		+	[[Category: Nuclear protein]]
		+	[[Category: Phosphorylation]]
		+	[[Category: Telomere]]

OCA: Protected "1w0u" [edit=sysop:move=sysop]

OCA — Wed, 16 Mar 2011 07:48:34 GMT

Protected "1w0u" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:48, 16 March 2011