5y59 - Revision history

OCA at 10:21, 27 March 2024

OCA — Wed, 27 Mar 2024 10:21:44 GMT

←Older revision		Revision as of 10:21, 27 March 2024
Line 1:		Line 1:

	==Crystal structure of Ku80 and Sir4==		==Crystal structure of Ku80 and Sir4==
-	<StructureSection load='5y59' size='340' side='right' caption='[[5y59]], [[Resolution\|resolution]] 2.40Å' scene=''>	+	<StructureSection load='5y59' size='340' side='right'caption='[[5y59]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5y59]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Baker's_yeast Baker's yeast~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y59 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5Y59 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5y59]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_VL3 Saccharomyces cerevisiae VL3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Y59 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.402Å</td></tr>
-	~~<tr~~ id~~='related'><td class~~="~~sblockLbl~~">~~<b>~~[[~~Related_structure~~\|~~Related:]]</b></td><td class="sblockDat">[[5y58\|5y58~~]]</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>YKU80, HDF2, YMR106C, YM9718.05C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~559292 Baker's yeast]), VL3_0944 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=764100 Baker's yeast])</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=5y59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y59 OCA], [https://pdbe.org/5y59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5y59 RCSB], [https://www.ebi.ac.uk/pdbsum/5y59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5y59 ProSAT]</span></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[http://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12]~~ </~~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=5y59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y59 OCA], [~~http~~://pdbe.org/5y59 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5y59 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5y59 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5y59 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/KU80_YEAST KU80_YEAST]] Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Appears to have a role in recruitment of telomerase and CDC13 to the telomere and the subsequent telomere elongation. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. KU70, of the KU70/KU80 heterodimer, binds to the stem loop of TLC1, the RNA component of telomerase. Involved in telomere maintenance. Interacts with telomeric repeats and subtelomeric sequences thereby controlling telomere length and protecting against subtelomeric rearrangement. Maintains telomeric chromatin, which is involved in silencing the expression of genes located at the telomere. Required for mating-type switching.<ref>PMID:10675560</ref> <ref>PMID:11046137</ref> <ref>PMID:12138180</ref> <ref>PMID:12975323</ref> <ref>PMID:14551211</ref> <ref>PMID:14585978</ref> <ref>PMID:16166630</ref> <ref>PMID:8910371</ref> <ref>PMID:8972848</ref> <ref>PMID:9563951</ref> <ref>PMID:9635192</ref> <ref>PMID:9635193</ref> <ref>PMID:9663392</ref> <ref>PMID:9914366</ref>	+	[https://www.uniprot.org/uniprot/KU80_YEAST KU80_YEAST] Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Appears to have a role in recruitment of telomerase and CDC13 to the telomere and the subsequent telomere elongation. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. KU70, of the KU70/KU80 heterodimer, binds to the stem loop of TLC1, the RNA component of telomerase. Involved in telomere maintenance. Interacts with telomeric repeats and subtelomeric sequences thereby controlling telomere length and protecting against subtelomeric rearrangement. Maintains telomeric chromatin, which is involved in silencing the expression of genes located at the telomere. Required for mating-type switching.<ref>PMID:10675560</ref> <ref>PMID:11046137</ref> <ref>PMID:12138180</ref> <ref>PMID:12975323</ref> <ref>PMID:14551211</ref> <ref>PMID:14585978</ref> <ref>PMID:16166630</ref> <ref>PMID:8910371</ref> <ref>PMID:8972848</ref> <ref>PMID:9563951</ref> <ref>PMID:9635192</ref> <ref>PMID:9635193</ref> <ref>PMID:9663392</ref> <ref>PMID:9914366</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Telomerase maintains chromosome ends from humans to yeasts. Recruitment of yeast telomerase to telomeres occurs through its Ku and Est1 subunits via independent interactions with telomerase RNA (TLC1) and telomeric proteins Sir4 and Cdc13, respectively. However, the structures of the molecules comprising these telomerase-recruiting pathways remain unknown. Here, we report crystal structures of the Ku heterodimer and Est1 complexed with their key binding partners. Two major findings are as follows: (1) Ku specifically binds to telomerase RNA in a distinct, yet related, manner to how it binds DNA; and (2) Est1 employs two separate pockets to bind distinct motifs of Cdc13. The N-terminal Cdc13-binding site of Est1 cooperates with the TLC1-Ku-Sir4 pathway for telomerase recruitment, whereas the C-terminal interface is dispensable for binding Est1 in vitro yet is nevertheless essential for telomere maintenance in vivo. Overall, our results integrate previous models and provide fundamentally valuable structural information regarding telomere biology.	+

-	Structural Insights into Yeast Telomerase Recruitment to Telomeres.,Chen H, Xue J, Churikov D, Hass EP, Shi S, Lemon LD, Luciano P, Bertuch AA, Zappulla DC, Geli V, Wu J, Lei M Cell. 2018 Jan 11;172(1-2):331-343.e13. doi: 10.1016/j.cell.2017.12.008. Epub, 2017 Dec 28. PMID:29290466<ref>PMID:29290466</ref>	+	==See Also==
-		+	*[[Helicase 3D structures\|Helicase 3D structures]]
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class~~=~~"pdbe-citations 5y59" style~~=~~"background-color:#fffaf0;"></div>~~	+
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Baker's yeast~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~DNA helicase~~]]	+	[[Category: Saccharomyces cerevisiae S288C]]
-	[[Category: Chen, H]]	+	[[Category: Saccharomyces cerevisiae VL3]]
-	[[Category: Lei, M]]	+	[[Category: Chen H]]
-	[[Category: Wu, J]]	+	[[Category: Lei M]]
-	[[Category: Xue, J]]	+	[[Category: Wu J]]
-	~~[[Category: Protein binding]]~~	+	[[Category: Xue J]]
-	~~[[Category: Protein-protein complex]]~~	+
-	~~[[Category: Telomerase]]~~	+
-	~~[[Category: Telomere~~]]	+

OCA at 06:46, 7 February 2018

OCA — Wed, 07 Feb 2018 06:46:42 GMT

←Older revision		Revision as of 06:46, 7 February 2018
Line 3:		Line 3:
	<StructureSection load='5y59' size='340' side='right' caption='[[5y59]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='5y59' size='340' side='right' caption='[[5y59]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5y59]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y59 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y59 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5y59]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y59 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y59 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5y58\|5y58]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5y58\|5y58]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">YKU80, HDF2, YMR106C, YM9718.05C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), VL3_0944 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=764100 Baker's yeast])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </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=5y59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y59 OCA], [http://pdbe.org/5y59 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y59 RCSB], [http://www.ebi.ac.uk/pdbsum/5y59 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y59 ProSAT]</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=5y59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y59 OCA], [http://pdbe.org/5y59 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y59 RCSB], [http://www.ebi.ac.uk/pdbsum/5y59 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y59 ProSAT]</span></td></tr>
Line 11:		Line 12:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/KU80_YEAST KU80_YEAST]] Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Appears to have a role in recruitment of telomerase and CDC13 to the telomere and the subsequent telomere elongation. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. KU70, of the KU70/KU80 heterodimer, binds to the stem loop of TLC1, the RNA component of telomerase. Involved in telomere maintenance. Interacts with telomeric repeats and subtelomeric sequences thereby controlling telomere length and protecting against subtelomeric rearrangement. Maintains telomeric chromatin, which is involved in silencing the expression of genes located at the telomere. Required for mating-type switching.<ref>PMID:10675560</ref> <ref>PMID:11046137</ref> <ref>PMID:12138180</ref> <ref>PMID:12975323</ref> <ref>PMID:14551211</ref> <ref>PMID:14585978</ref> <ref>PMID:16166630</ref> <ref>PMID:8910371</ref> <ref>PMID:8972848</ref> <ref>PMID:9563951</ref> <ref>PMID:9635192</ref> <ref>PMID:9635193</ref> <ref>PMID:9663392</ref> <ref>PMID:9914366</ref>		[[http://www.uniprot.org/uniprot/KU80_YEAST KU80_YEAST]] Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Appears to have a role in recruitment of telomerase and CDC13 to the telomere and the subsequent telomere elongation. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. KU70, of the KU70/KU80 heterodimer, binds to the stem loop of TLC1, the RNA component of telomerase. Involved in telomere maintenance. Interacts with telomeric repeats and subtelomeric sequences thereby controlling telomere length and protecting against subtelomeric rearrangement. Maintains telomeric chromatin, which is involved in silencing the expression of genes located at the telomere. Required for mating-type switching.<ref>PMID:10675560</ref> <ref>PMID:11046137</ref> <ref>PMID:12138180</ref> <ref>PMID:12975323</ref> <ref>PMID:14551211</ref> <ref>PMID:14585978</ref> <ref>PMID:16166630</ref> <ref>PMID:8910371</ref> <ref>PMID:8972848</ref> <ref>PMID:9563951</ref> <ref>PMID:9635192</ref> <ref>PMID:9635193</ref> <ref>PMID:9663392</ref> <ref>PMID:9914366</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Telomerase maintains chromosome ends from humans to yeasts. Recruitment of yeast telomerase to telomeres occurs through its Ku and Est1 subunits via independent interactions with telomerase RNA (TLC1) and telomeric proteins Sir4 and Cdc13, respectively. However, the structures of the molecules comprising these telomerase-recruiting pathways remain unknown. Here, we report crystal structures of the Ku heterodimer and Est1 complexed with their key binding partners. Two major findings are as follows: (1) Ku specifically binds to telomerase RNA in a distinct, yet related, manner to how it binds DNA; and (2) Est1 employs two separate pockets to bind distinct motifs of Cdc13. The N-terminal Cdc13-binding site of Est1 cooperates with the TLC1-Ku-Sir4 pathway for telomerase recruitment, whereas the C-terminal interface is dispensable for binding Est1 in vitro yet is nevertheless essential for telomere maintenance in vivo. Overall, our results integrate previous models and provide fundamentally valuable structural information regarding telomere biology.
		+
		+	Structural Insights into Yeast Telomerase Recruitment to Telomeres.,Chen H, Xue J, Churikov D, Hass EP, Shi S, Lemon LD, Luciano P, Bertuch AA, Zappulla DC, Geli V, Wu J, Lei M Cell. 2018 Jan 11;172(1-2):331-343.e13. doi: 10.1016/j.cell.2017.12.008. Epub, 2017 Dec 28. PMID:29290466<ref>PMID:29290466</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5y59" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Baker's yeast]]
	[[Category: DNA helicase]]		[[Category: DNA helicase]]
	[[Category: Chen, H]]		[[Category: Chen, H]]

OCA at 06:22, 20 December 2017

OCA — Wed, 20 Dec 2017 06:22:03 GMT

←Older revision		Revision as of 06:22, 20 December 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5y59 is ~~ON HOLD until Paper Publication~~	+	==Crystal structure of Ku80 and Sir4==
-		+	<StructureSection load='5y59' size='340' side='right' caption='[[5y59]], [[Resolution\|resolution]] 2.40Å' scene=''>
-	~~Authors~~: ~~Chen~~, H., ~~Xue~~, J., Wu, J., ~~Lei, M~~.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5y59]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y59 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y59 FirstGlance]. <br>
-	~~Description~~: ~~Crystal structure~~ of ~~Ku80~~ and ~~Sir4~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5y58\|5y58]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </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=5y59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y59 OCA], [http://pdbe.org/5y59 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y59 RCSB], [http://www.ebi.ac.uk/pdbsum/5y59 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y59 ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/KU80_YEAST KU80_YEAST]] Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Appears to have a role in recruitment of telomerase and CDC13 to the telomere and the subsequent telomere elongation. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. KU70, of the KU70/KU80 heterodimer, binds to the stem loop of TLC1, the RNA component of telomerase. Involved in telomere maintenance. Interacts with telomeric repeats and subtelomeric sequences thereby controlling telomere length and protecting against subtelomeric rearrangement. Maintains telomeric chromatin, which is involved in silencing the expression of genes located at the telomere. Required for mating-type switching.<ref>PMID:10675560</ref> <ref>PMID:11046137</ref> <ref>PMID:12138180</ref> <ref>PMID:12975323</ref> <ref>PMID:14551211</ref> <ref>PMID:14585978</ref> <ref>PMID:16166630</ref> <ref>PMID:8910371</ref> <ref>PMID:8972848</ref> <ref>PMID:9563951</ref> <ref>PMID:9635192</ref> <ref>PMID:9635193</ref> <ref>PMID:9663392</ref> <ref>PMID:9914366</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: DNA helicase]]
		+	[[Category: Chen, H]]
	[[Category: Lei, M]]		[[Category: Lei, M]]
		+	[[Category: Wu, J]]
	[[Category: Xue, J]]		[[Category: Xue, J]]
-	[[Category: ~~Chen, H~~]]	+	[[Category: Protein binding]]
-	[[Category: ~~Wu, J~~]]	+	[[Category: Protein-protein complex]]
		+	[[Category: Telomerase]]
		+	[[Category: Telomere]]

OCA: Protected "5y59" [edit=sysop:move=sysop]

OCA — Wed, 27 Sep 2017 16:09:11 GMT

Protected "5y59" [edit=sysop:move=sysop]

←Older revision

Revision as of 16:09, 27 September 2017

OCA: New page: '''Unreleased structure''' The entry 5y59 is ON HOLD until Paper Publication Authors: Chen, H., Xue, J., Wu, J., Lei, M. Description: Crystal structure of Ku80 and Sir4 [[Category: Unr...

OCA — Wed, 27 Sep 2017 16:09:10 GMT

New page: '''Unreleased structure''' The entry 5y59 is ON HOLD until Paper Publication Authors: Chen, H., Xue, J., Wu, J., Lei, M. Description: Crystal structure of Ku80 and Sir4 [[Category: Unr...

New page

'''Unreleased structure'''

The entry 5y59 is ON HOLD until Paper Publication

Authors: Chen, H., Xue, J., Wu, J., Lei, M.

Description: Crystal structure of Ku80 and Sir4
[[Category: Unreleased Structures]]
[[Category: Lei, M]]
[[Category: Xue, J]]
[[Category: Chen, H]]
[[Category: Wu, J]]