4ext - Revision history

OCA at 08:50, 20 March 2024

2024-03-20T08:50:19Z

← Older revision		Revision as of 08:50, 20 March 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4ext]] 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=4EXT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EXT FirstGlance]. <br>		<table><tr><td colspan='2'>[[4ext]] 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=4EXT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EXT FirstGlance]. <br>
	</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=4ext FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ext OCA], [https://pdbe.org/4ext PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ext RCSB], [https://www.ebi.ac.uk/pdbsum/4ext PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ext ProSAT]</span></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'>[https://proteopedia.org/fgij/fg.htm?mol=4ext FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ext OCA], [https://pdbe.org/4ext PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ext RCSB], [https://www.ebi.ac.uk/pdbsum/4ext PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ext ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/MD2L2_HUMAN MD2L2_HUMAN] Adapter protein able to interact with different proteins and involved in different biological processes. Mediates the interaction between the error-prone DNA polymerase zeta catalytic subunit REV3L and the inserter polymerase REV1, thereby mediating the second polymerase switching in translesion DNA synthesis. Translesion DNA synthesis releases the replication blockade of replicative polymerases, stalled in presence of DNA lesions. May also regulate another aspect of cellular response to DNA damage through regulation of the JNK-mediated phosphorylation and activation of the transcriptional activator ELK1. Inhibits the FZR1- and probably CDC20-mediated activation of the anaphase promoting complex APC thereby regulating progression through the cell cycle. Regulates TCF7L2-mediated gene transcription and may play a role in epithelial-mesenchymal transdifferentiation.<ref>PMID:11459825</ref> <ref>PMID:11459826</ref> <ref>PMID:17719540</ref> <ref>PMID:17296730</ref> <ref>PMID:19443654</ref>		[https://www.uniprot.org/uniprot/MD2L2_HUMAN MD2L2_HUMAN] Adapter protein able to interact with different proteins and involved in different biological processes. Mediates the interaction between the error-prone DNA polymerase zeta catalytic subunit REV3L and the inserter polymerase REV1, thereby mediating the second polymerase switching in translesion DNA synthesis. Translesion DNA synthesis releases the replication blockade of replicative polymerases, stalled in presence of DNA lesions. May also regulate another aspect of cellular response to DNA damage through regulation of the JNK-mediated phosphorylation and activation of the transcriptional activator ELK1. Inhibits the FZR1- and probably CDC20-mediated activation of the anaphase promoting complex APC thereby regulating progression through the cell cycle. Regulates TCF7L2-mediated gene transcription and may play a role in epithelial-mesenchymal transdifferentiation.<ref>PMID:11459825</ref> <ref>PMID:11459826</ref> <ref>PMID:17719540</ref> <ref>PMID:17296730</ref> <ref>PMID:19443654</ref>

			==See Also==
			*[[DNA polymerase 3D structures\|DNA polymerase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 04:21, 7 October 2022

2022-10-07T04:21:48Z

← Older revision		Revision as of 04:21, 7 October 2022
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	==Structure of polymerase-interacting domain of human Rev1 in complex with translesional synthesis polymerase zeta==		==Structure of polymerase-interacting domain of human Rev1 in complex with translesional synthesis polymerase zeta==
	<StructureSection load='4ext' size='340' side='right' caption='[[4ext]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='4ext' size='340' side='right'caption='[[4ext]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4ext]] 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=4EXT OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4EXT FirstGlance]. <br>		<table><tr><td colspan='2'>[[4ext]] 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=4EXT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EXT FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">REV1, REV1L ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), REV3L, POLZ, REV3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), MAD2L2, MAD2B, REV7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		</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=4ext FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ext OCA], [https://pdbe.org/4ext PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ext RCSB], [https://www.ebi.ac.uk/pdbsum/4ext PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ext 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=4ext FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ext OCA], [~~http~~://pdbe.org/4ext PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4ext RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4ext PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4ext ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/REV1_HUMAN REV1_HUMAN]] Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents.<ref>PMID:10536157</ref> <ref>PMID:10760286</ref> <ref>PMID:11278384</ref> <ref>PMID:11485998</ref> <ref>PMID:22266823</ref> [[http://www.uniprot.org/uniprot/MD2L2_HUMAN MD2L2_HUMAN]] Adapter protein able to interact with different proteins and involved in different biological processes. Mediates the interaction between the error-prone DNA polymerase zeta catalytic subunit REV3L and the inserter polymerase REV1, thereby mediating the second polymerase switching in translesion DNA synthesis. Translesion DNA synthesis releases the replication blockade of replicative polymerases, stalled in presence of DNA lesions. May also regulate another aspect of cellular response to DNA damage through regulation of the JNK-mediated phosphorylation and activation of the transcriptional activator ELK1. Inhibits the FZR1- and probably CDC20-mediated activation of the anaphase promoting complex APC thereby regulating progression through the cell cycle. Regulates TCF7L2-mediated gene transcription and may play a role in epithelial-mesenchymal transdifferentiation.<ref>PMID:11459825</ref> <ref>PMID:11459826</ref> <ref>PMID:17719540</ref> <ref>PMID:17296730</ref> <ref>PMID:19443654</ref> ~~[[http://www.uniprot.org/uniprot/DPOLZ_HUMAN DPOLZ_HUMAN]] Interacts with MAD2L2 to form the error prone DNA polymerase zeta involved in translesion DNA synthesis.~~		[https://www.uniprot.org/uniprot/MD2L2_HUMAN MD2L2_HUMAN] Adapter protein able to interact with different proteins and involved in different biological processes. Mediates the interaction between the error-prone DNA polymerase zeta catalytic subunit REV3L and the inserter polymerase REV1, thereby mediating the second polymerase switching in translesion DNA synthesis. Translesion DNA synthesis releases the replication blockade of replicative polymerases, stalled in presence of DNA lesions. May also regulate another aspect of cellular response to DNA damage through regulation of the JNK-mediated phosphorylation and activation of the transcriptional activator ELK1. Inhibits the FZR1- and probably CDC20-mediated activation of the anaphase promoting complex APC thereby regulating progression through the cell cycle. Regulates TCF7L2-mediated gene transcription and may play a role in epithelial-mesenchymal transdifferentiation.<ref>PMID:11459825</ref> <ref>PMID:11459826</ref> <ref>PMID:17719540</ref> <ref>PMID:17296730</ref> <ref>PMID:19443654</ref>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Human~~]]		[[Category: Homo sapiens]]
	[[Category: ~~Choi, B S~~]]		[[Category: Large Structures]]
	[[Category: ~~Ko, J S~~]]		[[Category: Choi BS]]
	[[Category: ~~Liu, D N~~]]		[[Category: Ko JS]]
	[[Category: ~~Ryu, K S~~]]		[[Category: Liu DN]]
	[[Category: ~~B-family polymerase]]~~		[[Category: Ryu KS]]
	~~[[Category: Dna damage tolerance]]~~
	~~[[Category: Polymerase-interacting domain]]~~
	~~[[Category: Rev1]]~~
	~~[[Category: Rev3]]~~
	~~[[Category: Rev7]]~~
	~~[[Category: Scaffold]]~~
	~~[[Category: Transferase-transcription complex]]~~
	~~[[Category: Translesional synthesis polymerase]]~~
	~~[[Category: Y-family polymerase~~]]

OCA at 01:58, 5 August 2016

2016-08-05T01:58:57Z

← Older revision		Revision as of 01:58, 5 August 2016
Line 1:		Line 1:

	==Structure of polymerase-interacting domain of human Rev1 in complex with translesional synthesis polymerase zeta==		==Structure of polymerase-interacting domain of human Rev1 in complex with translesional synthesis polymerase zeta==
	<StructureSection load='4ext' size='340' side='right' caption='[[4ext]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='4ext' size='340' side='right' caption='[[4ext]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4ext]] 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=4EXT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EXT FirstGlance]. <br>		<table><tr><td colspan='2'>[[4ext]] 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=4EXT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EXT FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">REV1, REV1L ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~]), REV3L, POLZ, REV3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~]), MAD2L2, MAD2B, REV7 ([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">REV1, REV1L ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), REV3L, POLZ, REV3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), MAD2L2, MAD2B, REV7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4ext FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ext OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ext RCSB], [http://www.ebi.ac.uk/pdbsum/4ext 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=4ext FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ext OCA], [http://pdbe.org/4ext PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ext RCSB], [http://www.ebi.ac.uk/pdbsum/4ext PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ext ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 12:		Line 13:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Homo sapiens~~]]		[[Category: Human]]
	[[Category: Choi, B S]]		[[Category: Choi, B S]]
	[[Category: Ko, J S]]		[[Category: Ko, J S]]

OCA at 21:49, 24 December 2014

2014-12-24T21:49:22Z

← Older revision		Revision as of 21:49, 24 December 2014
Line 1:		Line 1:
	~~{{STRUCTURE_4ext\| PDB=4ext \| SCENE= }}~~		==Structure of polymerase-interacting domain of human Rev1 in complex with translesional synthesis polymerase zeta==
	===Structure of polymerase-interacting domain of human Rev1 in complex with translesional synthesis polymerase zeta===		<StructureSection load='4ext' size='340' side='right' caption='[[4ext]], [[Resolution\|resolution]] 1.90Å' scene=''>
			== Structural highlights ==
	==Function==		<table><tr><td colspan='2'>[[4ext]] 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=4EXT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EXT FirstGlance]. <br>
			</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">REV1, REV1L ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), REV3L, POLZ, REV3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), MAD2L2, MAD2B, REV7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=4ext FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ext OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ext RCSB], [http://www.ebi.ac.uk/pdbsum/4ext PDBsum]</span></td></tr>
			</table>
			== Function ==
	[[http://www.uniprot.org/uniprot/REV1_HUMAN REV1_HUMAN]] Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents.<ref>PMID:10536157</ref> <ref>PMID:10760286</ref> <ref>PMID:11278384</ref> <ref>PMID:11485998</ref> <ref>PMID:22266823</ref> [[http://www.uniprot.org/uniprot/MD2L2_HUMAN MD2L2_HUMAN]] Adapter protein able to interact with different proteins and involved in different biological processes. Mediates the interaction between the error-prone DNA polymerase zeta catalytic subunit REV3L and the inserter polymerase REV1, thereby mediating the second polymerase switching in translesion DNA synthesis. Translesion DNA synthesis releases the replication blockade of replicative polymerases, stalled in presence of DNA lesions. May also regulate another aspect of cellular response to DNA damage through regulation of the JNK-mediated phosphorylation and activation of the transcriptional activator ELK1. Inhibits the FZR1- and probably CDC20-mediated activation of the anaphase promoting complex APC thereby regulating progression through the cell cycle. Regulates TCF7L2-mediated gene transcription and may play a role in epithelial-mesenchymal transdifferentiation.<ref>PMID:11459825</ref> <ref>PMID:11459826</ref> <ref>PMID:17719540</ref> <ref>PMID:17296730</ref> <ref>PMID:19443654</ref> [[http://www.uniprot.org/uniprot/DPOLZ_HUMAN DPOLZ_HUMAN]] Interacts with MAD2L2 to form the error prone DNA polymerase zeta involved in translesion DNA synthesis.		[[http://www.uniprot.org/uniprot/REV1_HUMAN REV1_HUMAN]] Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents.<ref>PMID:10536157</ref> <ref>PMID:10760286</ref> <ref>PMID:11278384</ref> <ref>PMID:11485998</ref> <ref>PMID:22266823</ref> [[http://www.uniprot.org/uniprot/MD2L2_HUMAN MD2L2_HUMAN]] Adapter protein able to interact with different proteins and involved in different biological processes. Mediates the interaction between the error-prone DNA polymerase zeta catalytic subunit REV3L and the inserter polymerase REV1, thereby mediating the second polymerase switching in translesion DNA synthesis. Translesion DNA synthesis releases the replication blockade of replicative polymerases, stalled in presence of DNA lesions. May also regulate another aspect of cellular response to DNA damage through regulation of the JNK-mediated phosphorylation and activation of the transcriptional activator ELK1. Inhibits the FZR1- and probably CDC20-mediated activation of the anaphase promoting complex APC thereby regulating progression through the cell cycle. Regulates TCF7L2-mediated gene transcription and may play a role in epithelial-mesenchymal transdifferentiation.<ref>PMID:11459825</ref> <ref>PMID:11459826</ref> <ref>PMID:17719540</ref> <ref>PMID:17296730</ref> <ref>PMID:19443654</ref> [[http://www.uniprot.org/uniprot/DPOLZ_HUMAN DPOLZ_HUMAN]] Interacts with MAD2L2 to form the error prone DNA polymerase zeta involved in translesion DNA synthesis.
			== References ==
	==~~About this Structure==~~		<references/>
	[[4ext]] 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=4EXT OCA].		__TOC__
			</StructureSection>
	~~==Reference~~==
	<references ~~group="xtra"~~/><~~references~~/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Choi, B S.]]		[[Category: Choi, B S]]
	[[Category: Ko, J S.]]		[[Category: Ko, J S]]
	[[Category: Liu, D N.]]		[[Category: Liu, D N]]
	[[Category: Ryu, K S.]]		[[Category: Ryu, K S]]
	[[Category: B-family polymerase]]		[[Category: B-family polymerase]]
	[[Category: Dna damage tolerance]]		[[Category: Dna damage tolerance]]

OCA at 07:49, 8 May 2013

2013-05-08T07:49:43Z

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+{{STRUCTURE_4ext|  PDB=4ext  |  SCENE=  }}
-The entry 4ext is ON HOLD  until Paper Publication
+==Function==
-Authors: Liu, D.N., Ryu, K.S., Ko, J.S., Choi, B.S.
+==About this Structure==
-Description: Structure of polymerase-interacting domain of human Rev1 in complex with translesional synthesis polymerase zeta
+==Reference==

OCA at 05:39, 3 October 2012

2012-10-03T05:39:57Z

← Older revision		Revision as of 05:39, 3 October 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4ext is ON HOLD		The entry 4ext is ON HOLD until Paper Publication

	Authors: Liu, D.N., Ryu, K.S., Ko, J.S., Choi, B.S.		Authors: Liu, D.N., Ryu, K.S., Ko, J.S., Choi, B.S.

	Description: Structure of polymerase-interacting domain of human Rev1 in complex with translesional synthesis polymerase zeta		Description: Structure of polymerase-interacting domain of human Rev1 in complex with translesional synthesis polymerase zeta

OCA at 05:29, 30 May 2012

2012-05-30T05:29:47Z

← Older revision		Revision as of 05:29, 30 May 2012
Line 3:		Line 3:
	The entry 4ext is ON HOLD		The entry 4ext is ON HOLD

	Authors: Liu,D.N., Ryu,K.S., Ko,J.S., Choi,B.S.		Authors: Liu, D.N., Ryu, K.S., Ko, J.S., Choi, B.S.

	Description: Structure of polymerase-interacting domain of human Rev1 in complex with translesional synthesis polymerase zeta		Description: Structure of polymerase-interacting domain of human Rev1 in complex with translesional synthesis polymerase zeta

OCA: Protected "4ext" [edit=sysop:move=sysop]

2012-05-09T08:53:08Z

Protected "4ext" [edit=sysop:move=sysop]

← Older revision	Revision as of 08:53, 9 May 2012
(No difference)

OCA: New page: '''Unreleased structure''' The entry 4ext is ON HOLD Authors: Liu,D.N., Ryu,K.S., Ko,J.S., Choi,B.S. Description: Structure of polymerase-interacting domain of human Rev1 in complex wi...

2012-05-09T08:53:07Z

New page: '''Unreleased structure''' The entry 4ext is ON HOLD Authors: Liu,D.N., Ryu,K.S., Ko,J.S., Choi,B.S. Description: Structure of polymerase-interacting domain of human Rev1 in complex wi...

New page

'''Unreleased structure'''

The entry 4ext is ON HOLD

Authors: Liu,D.N., Ryu,K.S., Ko,J.S., Choi,B.S.

Description: Structure of polymerase-interacting domain of human Rev1 in complex with translesional synthesis polymerase zeta