4ea5 - Revision history

OCA at 14:56, 14 March 2024

2024-03-14T14:56:31Z

← Older revision		Revision as of 14:56, 14 March 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4ea5]] 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=4EA5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EA5 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4ea5]] 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=4EA5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EA5 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5HU:5-HYDROXYMETHYLURIDINE-2-DEOXY-5-MONOPHOSPHATE'>5HU</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]] 2.14Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5HU:5-HYDROXYMETHYLURIDINE-2-DEOXY-5-MONOPHOSPHATE'>5HU</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=4ea5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ea5 OCA], [https://pdbe.org/4ea5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ea5 RCSB], [https://www.ebi.ac.uk/pdbsum/4ea5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ea5 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=4ea5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ea5 OCA], [https://pdbe.org/4ea5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ea5 RCSB], [https://www.ebi.ac.uk/pdbsum/4ea5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ea5 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/MBD4_HUMAN MBD4_HUMAN]] Mismatch-specific DNA N-glycosylase involved in DNA repair. Has thymine glycosylase activity and is specific for G:T mismatches within methylated and unmethylated CpG sites. Can also remove uracil or 5-fluorouracil in G:U mismatches. Has no lyase activity. Was first identified as methyl-CpG-binding protein.<ref>PMID:10097147</ref> <ref>PMID:10930409</ref>		[https://www.uniprot.org/uniprot/MBD4_HUMAN MBD4_HUMAN] Mismatch-specific DNA N-glycosylase involved in DNA repair. Has thymine glycosylase activity and is specific for G:T mismatches within methylated and unmethylated CpG sites. Can also remove uracil or 5-fluorouracil in G:U mismatches. Has no lyase activity. Was first identified as methyl-CpG-binding protein.<ref>PMID:10097147</ref> <ref>PMID:10930409</ref>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	Active DNA demethylation in mammals occurs via hydroxylation of 5-methylcytosine to 5-hydroxymethylcytosine (5hmC) by the ten-eleven translocation family of proteins (TETs). 5hmC residues in DNA can be further oxidized by TETs to 5-carboxylcytosines and/or deaminated by the Activation Induced Deaminase/Apolipoprotein B mRNA-editing enzyme complex family proteins to 5-hydromethyluracil (5hmU). Excision and replacement of these intermediates is initiated by DNA glycosylases such as thymine-DNA glycosylase (TDG), methyl-binding domain protein 4 (MBD4) and single-strand specific monofunctional uracil-DNA glycosylase 1 in the base excision repair pathway. Here, we report detailed biochemical and structural characterization of human MBD4 which contains mismatch-specific TDG activity. Full-length as well as catalytic domain (residues 426-580) of human MBD4 (MBD4(cat)) can remove 5hmU when opposite to G with good efficiency. Here, we also report six crystal structures of human MBD4(cat): an unliganded form and five binary complexes with duplex DNA containing a TG, 5hmUG or AP*G (apurinic/apyrimidinic) mismatch at the target base pair. These structures reveal that MBD4(cat) uses a base flipping mechanism to specifically recognize thymine and 5hmU. The recognition mechanism of flipped-out 5hmU bases in MBD4(cat) active site supports the potential role of MBD4, together with TDG, in maintenance of genome stability and active DNA demethylation in mammals.

	Biochemical and structural characterization of the glycosylase domain of MBD4 bound to thymine and 5-hydroxymethyuracil-containing DNA.,Morera S, Grin I, Vigouroux A, Couve S, Henriot V, Saparbaev M, Ishchenko AA Nucleic Acids Res. 2012 Jul 30. PMID:22848106<ref>PMID:22848106</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 4ea5" style="background-color:#fffaf0;"></div~~>

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

OCA at 06:59, 28 September 2022

2022-09-28T06:59:41Z

← Older revision		Revision as of 06:59, 28 September 2022
Line 1:		Line 1:

	==Structure of the glycoslyase domain of MBD4 bound to a 5hmU containing DNA==		==Structure of the glycoslyase domain of MBD4 bound to a 5hmU containing DNA==
	<StructureSection load='4ea5' size='340' side='right' caption='[[4ea5]], [[Resolution\|resolution]] 2.14Å' scene=''>		<StructureSection load='4ea5' size='340' side='right'caption='[[4ea5]], [[Resolution\|resolution]] 2.14Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4ea5]] 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=4EA5 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4EA5 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4ea5]] 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=4EA5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EA5 FirstGlance]. <br>
	</td></tr><tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=5HU:5-HYDROXYMETHYLURIDINE-2-DEOXY-5-MONOPHOSPHATE'>5HU</scene>~~</td></tr>~~		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5HU:5-HYDROXYMETHYLURIDINE-2-DEOXY-5-MONOPHOSPHATE'>5HU</scene></td></tr>
	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4e9e\|4e9e]], [[4e9f\|4e9f]], [[4e9g\|4e9g]], [[4e9h\|4e9h]], [[4ea4\|4ea4]]</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=4ea5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ea5 OCA], [https://pdbe.org/4ea5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ea5 RCSB], [https://www.ebi.ac.uk/pdbsum/4ea5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ea5 ProSAT]</span></td></tr>
	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MBD4, MED1 ([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=4ea5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ea5 OCA], [~~http~~://pdbe.org/4ea5 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4ea5 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4ea5 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4ea5 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/MBD4_HUMAN MBD4_HUMAN]] Mismatch-specific DNA N-glycosylase involved in DNA repair. Has thymine glycosylase activity and is specific for G:T mismatches within methylated and unmethylated CpG sites. Can also remove uracil or 5-fluorouracil in G:U mismatches. Has no lyase activity. Was first identified as methyl-CpG-binding protein.<ref>PMID:10097147</ref> <ref>PMID:10930409</ref>		[[https://www.uniprot.org/uniprot/MBD4_HUMAN MBD4_HUMAN]] Mismatch-specific DNA N-glycosylase involved in DNA repair. Has thymine glycosylase activity and is specific for G:T mismatches within methylated and unmethylated CpG sites. Can also remove uracil or 5-fluorouracil in G:U mismatches. Has no lyase activity. Was first identified as methyl-CpG-binding protein.<ref>PMID:10097147</ref> <ref>PMID:10930409</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 20:

	==See Also==		==See Also==
	*[[Methyl CpG binding protein\|Methyl CpG binding protein]]		*[[Methyl CpG binding protein 3D structures\|Methyl CpG binding protein 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Human~~]]		[[Category: Homo sapiens]]
	[[Category: ~~Morera, S~~]]		[[Category: Large Structures]]
	[[Category: ~~Vigouroux, A~~]]		[[Category: Morera S]]
	[[Category: ~~Hhh dna glycosylase family]]~~		[[Category: Vigouroux A]]
	~~[[Category: Hydrolase-dna complex~~]]

OCA at 17:18, 4 August 2016

2016-08-04T17:18:11Z

← Older revision		Revision as of 17:18, 4 August 2016
Line 1:		Line 1:

	==Structure of the glycoslyase domain of MBD4 bound to a 5hmU containing DNA==		==Structure of the glycoslyase domain of MBD4 bound to a 5hmU containing DNA==
	<StructureSection load='4ea5' size='340' side='right' caption='[[4ea5]], [[Resolution\|resolution]] 2.14Å' scene=''>		<StructureSection load='4ea5' size='340' side='right' caption='[[4ea5]], [[Resolution\|resolution]] 2.14Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4ea5]] 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=4EA5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EA5 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4ea5]] 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=4EA5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EA5 FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=5HU:5-HYDROXYMETHYLURIDINE-2-DEOXY-5-MONOPHOSPHATE'>5HU</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=5HU:5-HYDROXYMETHYLURIDINE-2-DEOXY-5-MONOPHOSPHATE'>5HU</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4e9e\|4e9e]], [[4e9f\|4e9f]], [[4e9g\|4e9g]], [[4e9h\|4e9h]], [[4ea4\|4ea4]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4e9e\|4e9e]], [[4e9f\|4e9f]], [[4e9g\|4e9g]], [[4e9h\|4e9h]], [[4ea4\|4ea4]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MBD4, MED1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MBD4, MED1 ([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=4ea5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ea5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ea5 RCSB], [http://www.ebi.ac.uk/pdbsum/4ea5 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=4ea5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ea5 OCA], [http://pdbe.org/4ea5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ea5 RCSB], [http://www.ebi.ac.uk/pdbsum/4ea5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ea5 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	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 4ea5" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 25:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Homo sapiens~~]]		[[Category: Human]]
	[[Category: Morera, S]]		[[Category: Morera, S]]
	[[Category: Vigouroux, A]]		[[Category: Vigouroux, A]]
	[[Category: Hhh dna glycosylase family]]		[[Category: Hhh dna glycosylase family]]
	[[Category: Hydrolase-dna complex]]		[[Category: Hydrolase-dna complex]]

OCA at 17:28, 24 December 2014

2014-12-24T17:28:46Z

← Older revision		Revision as of 17:28, 24 December 2014
Line 8:		Line 8:
	<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=4ea5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ea5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ea5 RCSB], [http://www.ebi.ac.uk/pdbsum/4ea5 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=4ea5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ea5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ea5 RCSB], [http://www.ebi.ac.uk/pdbsum/4ea5 PDBsum]</span></td></tr>
	</table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/MBD4_HUMAN MBD4_HUMAN]] Mismatch-specific DNA N-glycosylase involved in DNA repair. Has thymine glycosylase activity and is specific for G:T mismatches within methylated and unmethylated CpG sites. Can also remove uracil or 5-fluorouracil in G:U mismatches. Has no lyase activity. Was first identified as methyl-CpG-binding protein.<ref>PMID:10097147</ref> <ref>PMID:10930409</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 15:15, 9 December 2014

2014-12-09T15:15:32Z

← Older revision		Revision as of 15:15, 9 December 2014
Line 1:		Line 1:
	[[~~Image~~:~~4ea5~~.~~png~~\|~~left~~\|~~200px~~]]		==Structure of the glycoslyase domain of MBD4 bound to a 5hmU containing DNA==
			<StructureSection load='4ea5' size='340' side='right' caption='[[4ea5]], [[Resolution\|resolution]] 2.14Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[4ea5]] 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=4EA5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EA5 FirstGlance]. <br>
			</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=5HU:5-HYDROXYMETHYLURIDINE-2-DEOXY-5-MONOPHOSPHATE'>5HU</scene></td></tr>
			<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4e9e\|4e9e]], [[4e9f\|4e9f]], [[4e9g\|4e9g]], [[4e9h\|4e9h]], [[4ea4\|4ea4]]</td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MBD4, MED1 ([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=4ea5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ea5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ea5 RCSB], [http://www.ebi.ac.uk/pdbsum/4ea5 PDBsum]</span></td></tr>
			</table>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Active DNA demethylation in mammals occurs via hydroxylation of 5-methylcytosine to 5-hydroxymethylcytosine (5hmC) by the ten-eleven translocation family of proteins (TETs). 5hmC residues in DNA can be further oxidized by TETs to 5-carboxylcytosines and/or deaminated by the Activation Induced Deaminase/Apolipoprotein B mRNA-editing enzyme complex family proteins to 5-hydromethyluracil (5hmU). Excision and replacement of these intermediates is initiated by DNA glycosylases such as thymine-DNA glycosylase (TDG), methyl-binding domain protein 4 (MBD4) and single-strand specific monofunctional uracil-DNA glycosylase 1 in the base excision repair pathway. Here, we report detailed biochemical and structural characterization of human MBD4 which contains mismatch-specific TDG activity. Full-length as well as catalytic domain (residues 426-580) of human MBD4 (MBD4(cat)) can remove 5hmU when opposite to G with good efficiency. Here, we also report six crystal structures of human MBD4(cat): an unliganded form and five binary complexes with duplex DNA containing a TG, 5hmUG or AP*G (apurinic/apyrimidinic) mismatch at the target base pair. These structures reveal that MBD4(cat) uses a base flipping mechanism to specifically recognize thymine and 5hmU. The recognition mechanism of flipped-out 5hmU bases in MBD4(cat) active site supports the potential role of MBD4, together with TDG, in maintenance of genome stability and active DNA demethylation in mammals.

	~~{{STRUCTURE_4ea5\| PDB=4ea5 \| SCENE= }}~~		Biochemical and structural characterization of the glycosylase domain of MBD4 bound to thymine and 5-hydroxymethyuracil-containing DNA.,Morera S, Grin I, Vigouroux A, Couve S, Henriot V, Saparbaev M, Ishchenko AA Nucleic Acids Res. 2012 Jul 30. PMID:22848106<ref>PMID:22848106</ref>

	~~===Structure~~ of the ~~glycoslyase domain~~ of ~~MBD4 bound to a 5hmU containing DNA===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>

			==See Also==
	==~~About this Structure~~==		*[[Methyl CpG binding protein\|Methyl CpG binding protein]]
	[[~~4ea5~~]] 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=4EA5 OCA].		== References ==
			<references/>
	==~~Reference~~==		__TOC__
	<~~ref group="xtra">PMID:022848106<~~/~~ref~~><~~references group="xtra"~~/>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Morera, S.]]		[[Category: Morera, S]]
	[[Category: Vigouroux, A.]]		[[Category: Vigouroux, A]]
	[[Category: Hhh dna glycosylase family]]		[[Category: Hhh dna glycosylase family]]
	[[Category: Hydrolase-dna complex]]		[[Category: Hydrolase-dna complex]]

OCA at 14:13, 8 November 2012

2012-11-08T14:13:20Z

← Older revision		Revision as of 14:13, 8 November 2012
Line 1:		Line 1:
	[[Image:4ea5.~~jpg~~\|left\|200px]]		[[Image:4ea5.png\|left\|200px]]

	{{STRUCTURE_4ea5\| PDB=4ea5 \| SCENE= }}		{{STRUCTURE_4ea5\| PDB=4ea5 \| SCENE= }}
Line 5:		Line 5:
	===Structure of the glycoslyase domain of MBD4 bound to a 5hmU containing DNA===		===Structure of the glycoslyase domain of MBD4 bound to a 5hmU containing DNA===

	~~{{ABSTRACT_PUBMED_22848106}}~~

	==About this Structure==		==About this Structure==

OCA at 05:20, 8 August 2012

2012-08-08T05:20:05Z

← Older revision		Revision as of 05:20, 8 August 2012
Line 1:		Line 1:
	~~'''Unreleased structure'''~~		[[Image:4ea5.jpg\|left\|200px]]

	~~The entry~~ 4ea5 ~~is ON HOLD~~ ~~until Paper Publication~~		{{STRUCTURE_4ea5\| PDB=4ea5 \| SCENE= }}

	~~Authors: Morera, S., Vigouroux, A.~~		===Structure of the glycoslyase domain of MBD4 bound to a 5hmU containing DNA===

	~~Description:~~ Structure ~~of the glycoslyase domain of MBD4 bound to~~ a ~~5hmU containing DNA~~		{{ABSTRACT_PUBMED_22848106}}

			==About this Structure==
			[[4ea5]] 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=4EA5 OCA].

			==Reference==
			<ref group="xtra">PMID:022848106</ref><references group="xtra"/>
			[[Category: Homo sapiens]]
			[[Category: Morera, S.]]
			[[Category: Vigouroux, A.]]
			[[Category: Hhh dna glycosylase family]]
			[[Category: Hydrolase-dna complex]]

OCA at 06:40, 11 April 2012

2012-04-11T06:40:02Z

← Older revision		Revision as of 06:40, 11 April 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4ea5 is ON HOLD		The entry 4ea5 is ON HOLD until Paper Publication

	Authors: ~~morera~~, s, ~~vigouroux~~, a		Authors: Morera, S., Vigouroux, A.

	Description: Structure of the ~~glycsolyase~~ domain of MBD4 bound to a 5hmU containing DNA		Description: Structure of the glycoslyase domain of MBD4 bound to a 5hmU containing DNA

OCA: Protected "4ea5" [edit=sysop:move=sysop]

2012-03-28T07:26:20Z

Protected "4ea5" [edit=sysop:move=sysop]

← Older revision	Revision as of 07:26, 28 March 2012
(No difference)

OCA: New page: '''Unreleased structure''' The entry 4ea5 is ON HOLD Authors: morera, s, vigouroux, a Description: Structure of the glycsolyase domain of MBD4 bound to a 5hmU containing DNA

2012-03-28T07:26:19Z

New page: '''Unreleased structure''' The entry 4ea5 is ON HOLD Authors: morera, s, vigouroux, a Description: Structure of the glycsolyase domain of MBD4 bound to a 5hmU containing DNA

New page

'''Unreleased structure'''

The entry 4ea5 is ON HOLD

Authors: morera, s, vigouroux, a

Description: Structure of the glycsolyase domain of MBD4 bound to a 5hmU containing DNA