4e9e - Revision history

OCA at 14:56, 14 March 2024

2024-03-14T14:56:01Z

← Older revision		Revision as of 14:56, 14 March 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4e9e]] is a 1 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=4E9E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E9E FirstGlance]. <br>		<table><tr><td colspan='2'>[[4e9e]] is a 1 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=4E9E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E9E 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=4e9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e9e OCA], [https://pdbe.org/4e9e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e9e RCSB], [https://www.ebi.ac.uk/pdbsum/4e9e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e9e 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=4e9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e9e OCA], [https://pdbe.org/4e9e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e9e RCSB], [https://www.ebi.ac.uk/pdbsum/4e9e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e9e 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 4e9e" style="background-color:#fffaf0;"></div~~>

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

OCA at 06:58, 28 September 2022

2022-09-28T06:58:37Z

← Older revision		Revision as of 06:58, 28 September 2022
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	==Structure of the glycosylase domain of MBD4==		==Structure of the glycosylase domain of MBD4==
	<StructureSection load='4e9e' size='340' side='right' caption='[[4e9e]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='4e9e' size='340' side='right'caption='[[4e9e]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4e9e]] is a 1 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=4E9E OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4E9E FirstGlance]. <br>		<table><tr><td colspan='2'>[[4e9e]] is a 1 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=4E9E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E9E FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3iho\|3iho]], [[4e9f\|4e9f]], [[4e9g\|4e9g]], [[4e9h\|4e9h]], [[4ea4\|4ea4]], [[4eab\|4eab]]</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=4e9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e9e OCA], [https://pdbe.org/4e9e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e9e RCSB], [https://www.ebi.ac.uk/pdbsum/4e9e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e9e 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=4e9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e9e OCA], [~~http~~://pdbe.org/4e9e PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4e9e RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4e9e PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4e9e 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 21:		Line 19:

	==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 superfamily]]~~		[[Category: Vigouroux A]]
	~~[[Category: Hydrolase~~]]

OCA at 17:30, 5 August 2016

2016-08-05T17:30:51Z

← Older revision		Revision as of 17:30, 5 August 2016
Line 1:		Line 1:

	==Structure of the glycosylase domain of MBD4==		==Structure of the glycosylase domain of MBD4==
	<StructureSection load='4e9e' size='340' side='right' caption='[[4e9e]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='4e9e' size='340' side='right' caption='[[4e9e]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4e9e]] is a 1 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=4E9E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E9E FirstGlance]. <br>		<table><tr><td colspan='2'>[[4e9e]] is a 1 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=4E9E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E9E FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3iho\|3iho]], [[4e9f\|4e9f]], [[4e9g\|4e9g]], [[4e9h\|4e9h]], [[4ea4\|4ea4]], [[4eab\|4eab]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3iho\|3iho]], [[4e9f\|4e9f]], [[4e9g\|4e9g]], [[4e9h\|4e9h]], [[4ea4\|4ea4]], [[4eab\|4eab]]</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=4e9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e9e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e9e RCSB], [http://www.ebi.ac.uk/pdbsum/4e9e 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=4e9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e9e OCA], [http://pdbe.org/4e9e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4e9e RCSB], [http://www.ebi.ac.uk/pdbsum/4e9e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4e9e ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	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 4e9e" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 24:		Line 26:
	__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 superfamily]]		[[Category: Hhh dna glycosylase superfamily]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 20:39, 25 December 2014

2014-12-25T20:39:13Z

← Older revision		Revision as of 20:39, 25 December 2014
Line 7:		Line 7:
	<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=4e9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e9e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e9e RCSB], [http://www.ebi.ac.uk/pdbsum/4e9e 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=4e9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e9e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e9e RCSB], [http://www.ebi.ac.uk/pdbsum/4e9e 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 17:07, 9 December 2014

2014-12-09T17:07:05Z

← Older revision		Revision as of 17:07, 9 December 2014
Line 1:		Line 1:
	[[~~Image~~:~~4e9e~~.~~png~~\|~~left~~\|~~200px~~]]		==Structure of the glycosylase domain of MBD4==
			<StructureSection load='4e9e' size='340' side='right' caption='[[4e9e]], [[Resolution\|resolution]] 1.90Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[4e9e]] is a 1 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=4E9E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E9E FirstGlance]. <br>
			</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3iho\|3iho]], [[4e9f\|4e9f]], [[4e9g\|4e9g]], [[4e9h\|4e9h]], [[4ea4\|4ea4]], [[4eab\|4eab]]</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=4e9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e9e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e9e RCSB], [http://www.ebi.ac.uk/pdbsum/4e9e 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_4e9e\| PDB=4e9e \| 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 ~~glycosylase domain~~ of ~~MBD4===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>

	~~{{ABSTRACT_PUBMED_22848106}}~~		==See Also==
			*[[Methyl CpG binding protein\|Methyl CpG binding protein]]
	==~~About this Structure~~==		== References ==
	[[~~4e9e]] is a 1 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=4E9E OCA~~].		<references/>
			__TOC__
	==~~Reference~~==		</StructureSection>
	<~~ref group="xtra">PMID:022848106<~~/~~ref~~><~~references group="xtra"~~/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Morera, S.]]		[[Category: Morera, S]]
	[[Category: Vigouroux, A.]]		[[Category: Vigouroux, A]]
	[[Category: Hhh dna glycosylase superfamily]]		[[Category: Hhh dna glycosylase superfamily]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 10:45, 14 November 2012

2012-11-14T10:45:20Z

← Older revision		Revision as of 10:45, 14 November 2012
Line 5:		Line 5:
	===Structure of the glycosylase domain of MBD4===		===Structure of the glycosylase domain of MBD4===

			{{ABSTRACT_PUBMED_22848106}}

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

OCA at 14:12, 8 November 2012

2012-11-08T14:12:57Z

← Older revision		Revision as of 14:12, 8 November 2012
Line 1:		Line 1:
	[[Image:4e9e.~~jpg~~\|left\|200px]]		[[Image:4e9e.png\|left\|200px]]

	{{STRUCTURE_4e9e\| PDB=4e9e \| SCENE= }}		{{STRUCTURE_4e9e\| PDB=4e9e \| SCENE= }}
Line 5:		Line 5:
	===Structure of the glycosylase domain of MBD4===		===Structure of the glycosylase domain of MBD4===

	~~{{ABSTRACT_PUBMED_22848106}}~~

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

OCA at 05:23, 8 August 2012

2012-08-08T05:23:10Z

← Older revision		Revision as of 05:23, 8 August 2012
Line 1:		Line 1:
	~~'''Unreleased structure'''~~		[[Image:4e9e.jpg\|left\|200px]]

	~~The entry~~ 4e9e ~~is ON HOLD~~ ~~until Paper Publication~~		{{STRUCTURE_4e9e\| PDB=4e9e \| SCENE= }}

	~~Authors: Morera, S., Vigouroux, A.~~		===Structure of the glycosylase domain of MBD4===

	~~Description~~: ~~Structure of the~~ glycosylase ~~domain of MBD4~~		{{ABSTRACT_PUBMED_22848106}}

			==About this Structure==
			[[4e9e]] is a 1 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=4E9E OCA].

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

OCA at 06:39, 11 April 2012

2012-04-11T06:39:50Z

← Older revision		Revision as of 06:39, 11 April 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4e9e is ON HOLD		The entry 4e9e is ON HOLD until Paper Publication

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

	Description: Structure of the glycosylase domain of MBD4		Description: Structure of the glycosylase domain of MBD4

OCA: Protected "4e9e" [edit=sysop:move=sysop]

2012-03-28T07:25:31Z

Protected "4e9e" [edit=sysop:move=sysop]

← Older revision	Revision as of 07:25, 28 March 2012
(No difference)