2ld1 - Revision history

OCA at 06:55, 1 May 2024

OCA — Wed, 01 May 2024 06:55:14 GMT

←Older revision		Revision as of 06:55, 1 May 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2ld1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LD1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LD1 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2ld1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LD1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LD1 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2ld1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ld1 OCA], [https://pdbe.org/2ld1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ld1 RCSB], [https://www.ebi.ac.uk/pdbsum/2ld1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ld1 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=2ld1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ld1 OCA], [https://pdbe.org/2ld1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ld1 RCSB], [https://www.ebi.ac.uk/pdbsum/2ld1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ld1 ProSAT]</span></td></tr>
	</table>		</table>
Line 11:		Line 12:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/ATRX_HUMAN ATRX_HUMAN] Could be a global transcriptional regulator. Modifies gene expression by affecting chromatin. May be involved in brain development and facial morphogenesis.		[https://www.uniprot.org/uniprot/ATRX_HUMAN ATRX_HUMAN] Could be a global transcriptional regulator. Modifies gene expression by affecting chromatin. May be involved in brain development and facial morphogenesis.
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The chromatin-associated protein ATRX was originally identified because mutations in the ATRX gene cause a severe form of syndromal X-linked mental retardation associated with alpha-thalassemia. Half of all of the disease-associated missense mutations cluster in a cysteine-rich region in the N terminus of ATRX. This region was named the ATRX-DNMT3-DNMT3L (ADD) domain, based on sequence homology with a family of DNA methyltransferases. Here, we report the solution structure of the ADD domain of ATRX, which consists of an N-terminal GATA-like zinc finger, a plant homeodomain finger, and a long C-terminal alpha-helix that pack together to form a single globular domain. Interestingly, the alpha-helix of the GATA-like finger is exposed and highly basic, suggesting a DNA-binding function for ATRX. The disease-causing mutations fall into two groups: the majority affect buried residues and hence affect the structural integrity of the ADD domain; another group affects a cluster of surface residues, and these are likely to perturb a potential protein interaction site. The effects of individual point mutations on the folding state and stability of the ADD domain correlate well with the levels of mutant ATRX protein in patients, providing insights into the molecular pathophysiology of ATR-X syndrome.
-
-	Structural consequences of disease-causing mutations in the ATRX-DNMT3-DNMT3L (ADD) domain of the chromatin-associated protein ATRX.,Argentaro A, Yang JC, Chapman L, Kowalczyk MS, Gibbons RJ, Higgs DR, Neuhaus D, Rhodes D Proc Natl Acad Sci U S A. 2007 Jul 17;104(29):11939-44. Epub 2007 Jul 3. PMID:17609377<ref>PMID:17609377</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 2ld1" style="background-color:#fffaf0;"></div>

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

OCA at 10:53, 15 February 2023

OCA — Wed, 15 Feb 2023 10:53:35 GMT

←Older revision		Revision as of 10:53, 15 February 2023
Line 1:		Line 1:

	==Structures and chemical shift assignments for the ADD domain of the ATRX protein==		==Structures and chemical shift assignments for the ADD domain of the ATRX protein==
-	<StructureSection load='2ld1' size='340' side='right'caption='[[2ld1~~]], [[NMR_Ensembles_of_Models \| 34 NMR models~~]]' scene=''>	+	<StructureSection load='2ld1' size='340' side='right'caption='[[2ld1]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2ld1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LD1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LD1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2ld1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LD1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LD1 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ATRX, RAD54L, XH2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=2ld1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ld1 OCA], [https://pdbe.org/2ld1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ld1 RCSB], [https://www.ebi.ac.uk/pdbsum/2ld1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ld1 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=2ld1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ld1 OCA], [https://pdbe.org/2ld1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ld1 RCSB], [https://www.ebi.ac.uk/pdbsum/2ld1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ld1 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/ATRX_HUMAN ATRX_HUMAN]] Defects in ATRX are the cause of alpha-thalassemia mental retardation syndrome X-linked (ATRX) [MIM:[https://omim.org/entry/301040 301040]]. ATR-X is an X-linked disorder comprising severe psychomotor retardation, facial dysmorphism, urogenital abnormalities, and alpha-thalassemia. An essential phenotypic trait are hemoglobin H erythrocyte inclusions.<ref>PMID:8968741</ref> <ref>PMID:7697714</ref> <ref>PMID:9043863</ref> <ref>PMID:9326931</ref> <ref>PMID:10660327</ref> <ref>PMID:10417298</ref> <ref>PMID:10204841</ref> <ref>PMID:10995512</ref> <ref>PMID:12116232</ref> <ref>PMID:16955409</ref> Defects in ATRX are the cause of mental retardation syndromic X-linked with hypotonic facies syndrome type 1 (MRXSHF1) [MIM:[https://omim.org/entry/309580 309580]]; also called Carpenter-Waziri syndrome (CWS), Juberg-Marsidi syndrome (JMS), Smith-Fineman-Myers syndrome type 1 (SFM1). Clinical features include severe mental retardation, dysmorphic facies, and a highly skewed X-inactivation pattern in carrier women. Other more variable features include hypogonadism, deafness, renal anomalies, and mild skeletal defects.<ref>PMID:10751095</ref> <ref>PMID:8630485</ref> <ref>PMID:10398237</ref> <ref>PMID:11050622</ref> <ref>PMID:16222662</ref> <ref>PMID:15565397</ref> Defects in ATRX are a cause of alpha-thalassemia myelodysplasia syndrome (ATMDS) [MIM:[https://omim.org/entry/300448 300448]]. In this disorder, alpha-thalassemia occurs as an acquired abnormality in association with a multilineage myelodysplasia.<ref>PMID:12858175</ref>	+	[https://www.uniprot.org/uniprot/ATRX_HUMAN ATRX_HUMAN] Defects in ATRX are the cause of alpha-thalassemia mental retardation syndrome X-linked (ATRX) [MIM:[https://omim.org/entry/301040 301040]. ATR-X is an X-linked disorder comprising severe psychomotor retardation, facial dysmorphism, urogenital abnormalities, and alpha-thalassemia. An essential phenotypic trait are hemoglobin H erythrocyte inclusions.<ref>PMID:8968741</ref> <ref>PMID:7697714</ref> <ref>PMID:9043863</ref> <ref>PMID:9326931</ref> <ref>PMID:10660327</ref> <ref>PMID:10417298</ref> <ref>PMID:10204841</ref> <ref>PMID:10995512</ref> <ref>PMID:12116232</ref> <ref>PMID:16955409</ref> Defects in ATRX are the cause of mental retardation syndromic X-linked with hypotonic facies syndrome type 1 (MRXSHF1) [MIM:[https://omim.org/entry/309580 309580]; also called Carpenter-Waziri syndrome (CWS), Juberg-Marsidi syndrome (JMS), Smith-Fineman-Myers syndrome type 1 (SFM1). Clinical features include severe mental retardation, dysmorphic facies, and a highly skewed X-inactivation pattern in carrier women. Other more variable features include hypogonadism, deafness, renal anomalies, and mild skeletal defects.<ref>PMID:10751095</ref> <ref>PMID:8630485</ref> <ref>PMID:10398237</ref> <ref>PMID:11050622</ref> <ref>PMID:16222662</ref> <ref>PMID:15565397</ref> Defects in ATRX are a cause of alpha-thalassemia myelodysplasia syndrome (ATMDS) [MIM:[https://omim.org/entry/300448 300448]. In this disorder, alpha-thalassemia occurs as an acquired abnormality in association with a multilineage myelodysplasia.<ref>PMID:12858175</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/ATRX_HUMAN ATRX_HUMAN]] Could be a global transcriptional regulator. Modifies gene expression by affecting chromatin. May be involved in brain development and facial morphogenesis.	+	[https://www.uniprot.org/uniprot/ATRX_HUMAN ATRX_HUMAN] Could be a global transcriptional regulator. Modifies gene expression by affecting chromatin. May be involved in brain development and facial morphogenesis.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~DNA helicase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Neuhaus, D]]	+	[[Category: Neuhaus D]]
-	[[Category: Yang, J]]	+	[[Category: Yang J]]
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Metal binding protein~~]]	+

OCA at 10:08, 12 May 2021

OCA — Wed, 12 May 2021 10:08:38 GMT

←Older revision		Revision as of 10:08, 12 May 2021
Line 1:		Line 1:

	==Structures and chemical shift assignments for the ADD domain of the ATRX protein==		==Structures and chemical shift assignments for the ADD domain of the ATRX protein==
-	<StructureSection load='2ld1' size='340' side='right' caption='[[2ld1]], [[NMR_Ensembles_of_Models \| 34 NMR models]]' scene=''>	+	<StructureSection load='2ld1' size='340' side='right'caption='[[2ld1]], [[NMR_Ensembles_of_Models \| 34 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2ld1]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LD1 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2LD1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2ld1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LD1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LD1 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ATRX, RAD54L, XH2 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ATRX, RAD54L, XH2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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'>[https://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [https://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=2ld1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ld1 OCA], [~~http~~://pdbe.org/2ld1 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2ld1 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2ld1 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2ld1 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=2ld1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ld1 OCA], [https://pdbe.org/2ld1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ld1 RCSB], [https://www.ebi.ac.uk/pdbsum/2ld1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ld1 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/ATRX_HUMAN ATRX_HUMAN]] Defects in ATRX are the cause of alpha-thalassemia mental retardation syndrome X-linked (ATRX) [MIM:[~~http~~://omim.org/entry/301040 301040]]. ATR-X is an X-linked disorder comprising severe psychomotor retardation, facial dysmorphism, urogenital abnormalities, and alpha-thalassemia. An essential phenotypic trait are hemoglobin H erythrocyte inclusions.<ref>PMID:8968741</ref> <ref>PMID:7697714</ref> <ref>PMID:9043863</ref> <ref>PMID:9326931</ref> <ref>PMID:10660327</ref> <ref>PMID:10417298</ref> <ref>PMID:10204841</ref> <ref>PMID:10995512</ref> <ref>PMID:12116232</ref> <ref>PMID:16955409</ref> Defects in ATRX are the cause of mental retardation syndromic X-linked with hypotonic facies syndrome type 1 (MRXSHF1) [MIM:[~~http~~://omim.org/entry/309580 309580]]; also called Carpenter-Waziri syndrome (CWS), Juberg-Marsidi syndrome (JMS), Smith-Fineman-Myers syndrome type 1 (SFM1). Clinical features include severe mental retardation, dysmorphic facies, and a highly skewed X-inactivation pattern in carrier women. Other more variable features include hypogonadism, deafness, renal anomalies, and mild skeletal defects.<ref>PMID:10751095</ref> <ref>PMID:8630485</ref> <ref>PMID:10398237</ref> <ref>PMID:11050622</ref> <ref>PMID:16222662</ref> <ref>PMID:15565397</ref> Defects in ATRX are a cause of alpha-thalassemia myelodysplasia syndrome (ATMDS) [MIM:[~~http~~://omim.org/entry/300448 300448]]. In this disorder, alpha-thalassemia occurs as an acquired abnormality in association with a multilineage myelodysplasia.<ref>PMID:12858175</ref>	+	[[https://www.uniprot.org/uniprot/ATRX_HUMAN ATRX_HUMAN]] Defects in ATRX are the cause of alpha-thalassemia mental retardation syndrome X-linked (ATRX) [MIM:[https://omim.org/entry/301040 301040]]. ATR-X is an X-linked disorder comprising severe psychomotor retardation, facial dysmorphism, urogenital abnormalities, and alpha-thalassemia. An essential phenotypic trait are hemoglobin H erythrocyte inclusions.<ref>PMID:8968741</ref> <ref>PMID:7697714</ref> <ref>PMID:9043863</ref> <ref>PMID:9326931</ref> <ref>PMID:10660327</ref> <ref>PMID:10417298</ref> <ref>PMID:10204841</ref> <ref>PMID:10995512</ref> <ref>PMID:12116232</ref> <ref>PMID:16955409</ref> Defects in ATRX are the cause of mental retardation syndromic X-linked with hypotonic facies syndrome type 1 (MRXSHF1) [MIM:[https://omim.org/entry/309580 309580]]; also called Carpenter-Waziri syndrome (CWS), Juberg-Marsidi syndrome (JMS), Smith-Fineman-Myers syndrome type 1 (SFM1). Clinical features include severe mental retardation, dysmorphic facies, and a highly skewed X-inactivation pattern in carrier women. Other more variable features include hypogonadism, deafness, renal anomalies, and mild skeletal defects.<ref>PMID:10751095</ref> <ref>PMID:8630485</ref> <ref>PMID:10398237</ref> <ref>PMID:11050622</ref> <ref>PMID:16222662</ref> <ref>PMID:15565397</ref> Defects in ATRX are a cause of alpha-thalassemia myelodysplasia syndrome (ATMDS) [MIM:[https://omim.org/entry/300448 300448]]. In this disorder, alpha-thalassemia occurs as an acquired abnormality in association with a multilineage myelodysplasia.<ref>PMID:12858175</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/ATRX_HUMAN ATRX_HUMAN]] Could be a global transcriptional regulator. Modifies gene expression by affecting chromatin. May be involved in brain development and facial morphogenesis.	+	[[https://www.uniprot.org/uniprot/ATRX_HUMAN ATRX_HUMAN]] Could be a global transcriptional regulator. Modifies gene expression by affecting chromatin. May be involved in brain development and facial morphogenesis.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 24:

	==See Also==		==See Also==
-	*[[Helicase\|Helicase]]	+	*[[Helicase 3D structures\|Helicase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 31:		Line 31:
	[[Category: DNA helicase]]		[[Category: DNA helicase]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Neuhaus, D]]		[[Category: Neuhaus, D]]
	[[Category: Yang, J]]		[[Category: Yang, J]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Metal binding protein]]		[[Category: Metal binding protein]]

OCA at 19:37, 1 August 2018

OCA — Wed, 01 Aug 2018 19:37:20 GMT

←Older revision		Revision as of 19:37, 1 August 2018
Line 1:		Line 1:
		+
	==Structures and chemical shift assignments for the ADD domain of the ATRX protein==		==Structures and chemical shift assignments for the ADD domain of the ATRX protein==
	<StructureSection load='2ld1' size='340' side='right' caption='[[2ld1]], [[NMR_Ensembles_of_Models \| 34 NMR models]]' scene=''>		<StructureSection load='2ld1' size='340' side='right' caption='[[2ld1]], [[NMR_Ensembles_of_Models \| 34 NMR models]]' scene=''>
Line 6:		Line 7:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ATRX, RAD54L, XH2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ATRX, RAD54L, XH2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2ld1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ld1 OCA], [http://pdbe.org/2ld1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ld1 RCSB], [http://www.ebi.ac.uk/pdbsum/2ld1 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=2ld1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ld1 OCA], [http://pdbe.org/2ld1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ld1 RCSB], [http://www.ebi.ac.uk/pdbsum/2ld1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ld1 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==

OCA at 08:33, 10 September 2015

OCA — Thu, 10 Sep 2015 08:33:45 GMT

←Older revision		Revision as of 08:33, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='2ld1' size='340' side='right' caption='[[2ld1]], [[NMR_Ensembles_of_Models \| 34 NMR models]]' scene=''>		<StructureSection load='2ld1' size='340' side='right' caption='[[2ld1]], [[NMR_Ensembles_of_Models \| 34 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2ld1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LD1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LD1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2ld1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LD1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LD1 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ATRX, RAD54L, XH2 ([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">ATRX, RAD54L, XH2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2ld1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ld1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ld1 RCSB], [http://www.ebi.ac.uk/pdbsum/2ld1 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=2ld1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ld1 OCA], [http://pdbe.org/2ld1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ld1 RCSB], [http://www.ebi.ac.uk/pdbsum/2ld1 PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 20:		Line 20:
	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 2ld1" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 28:		Line 29:
	</StructureSection>		</StructureSection>
	[[Category: DNA helicase]]		[[Category: DNA helicase]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Neuhaus, D]]		[[Category: Neuhaus, D]]
	[[Category: Yang, J]]		[[Category: Yang, J]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Metal binding protein]]		[[Category: Metal binding protein]]

OCA at 12:04, 18 December 2014

OCA — Thu, 18 Dec 2014 12:04:13 GMT

←Older revision		Revision as of 12:04, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_2ld1\| PDB=2ld1 \| SCENE= }}~~	+	==Structures and chemical shift assignments for the ADD domain of the ATRX protein==
-	===Structures and chemical shift assignments for the ADD domain of the ATRX protein===	+	<StructureSection load='2ld1' size='340' side='right' caption='[[2ld1]], [[NMR_Ensembles_of_Models \| 34 NMR models]]' scene=''>
-	~~{{ABSTRACT_PUBMED_17609377}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2ld1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LD1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LD1 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ATRX, RAD54L, XH2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=2ld1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ld1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ld1 RCSB], [http://www.ebi.ac.uk/pdbsum/2ld1 PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/ATRX_HUMAN ATRX_HUMAN]] Defects in ATRX are the cause of alpha-thalassemia mental retardation syndrome X-linked (ATRX) [MIM:[http://omim.org/entry/301040 301040]]. ATR-X is an X-linked disorder comprising severe psychomotor retardation, facial dysmorphism, urogenital abnormalities, and alpha-thalassemia. An essential phenotypic trait are hemoglobin H erythrocyte inclusions.<ref>PMID:8968741</ref> <ref>PMID:7697714</ref> <ref>PMID:9043863</ref> <ref>PMID:9326931</ref> <ref>PMID:10660327</ref> <ref>PMID:10417298</ref> <ref>PMID:10204841</ref> <ref>PMID:10995512</ref> <ref>PMID:12116232</ref> <ref>PMID:16955409</ref> Defects in ATRX are the cause of mental retardation syndromic X-linked with hypotonic facies syndrome type 1 (MRXSHF1) [MIM:[http://omim.org/entry/309580 309580]]; also called Carpenter-Waziri syndrome (CWS), Juberg-Marsidi syndrome (JMS), Smith-Fineman-Myers syndrome type 1 (SFM1). Clinical features include severe mental retardation, dysmorphic facies, and a highly skewed X-inactivation pattern in carrier women. Other more variable features include hypogonadism, deafness, renal anomalies, and mild skeletal defects.<ref>PMID:10751095</ref> <ref>PMID:8630485</ref> <ref>PMID:10398237</ref> <ref>PMID:11050622</ref> <ref>PMID:16222662</ref> <ref>PMID:15565397</ref> Defects in ATRX are a cause of alpha-thalassemia myelodysplasia syndrome (ATMDS) [MIM:[http://omim.org/entry/300448 300448]]. In this disorder, alpha-thalassemia occurs as an acquired abnormality in association with a multilineage myelodysplasia.<ref>PMID:12858175</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ATRX_HUMAN ATRX_HUMAN]] Could be a global transcriptional regulator. Modifies gene expression by affecting chromatin. May be involved in brain development and facial morphogenesis.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The chromatin-associated protein ATRX was originally identified because mutations in the ATRX gene cause a severe form of syndromal X-linked mental retardation associated with alpha-thalassemia. Half of all of the disease-associated missense mutations cluster in a cysteine-rich region in the N terminus of ATRX. This region was named the ATRX-DNMT3-DNMT3L (ADD) domain, based on sequence homology with a family of DNA methyltransferases. Here, we report the solution structure of the ADD domain of ATRX, which consists of an N-terminal GATA-like zinc finger, a plant homeodomain finger, and a long C-terminal alpha-helix that pack together to form a single globular domain. Interestingly, the alpha-helix of the GATA-like finger is exposed and highly basic, suggesting a DNA-binding function for ATRX. The disease-causing mutations fall into two groups: the majority affect buried residues and hence affect the structural integrity of the ADD domain; another group affects a cluster of surface residues, and these are likely to perturb a potential protein interaction site. The effects of individual point mutations on the folding state and stability of the ADD domain correlate well with the levels of mutant ATRX protein in patients, providing insights into the molecular pathophysiology of ATR-X syndrome.

-	~~==Disease==~~	+	Structural consequences of disease-causing mutations in the ATRX-DNMT3-DNMT3L (ADD) domain of the chromatin-associated protein ATRX.,Argentaro A, Yang JC, Chapman L, Kowalczyk MS, Gibbons RJ, Higgs DR, Neuhaus D, Rhodes D Proc Natl Acad Sci U S A. 2007 Jul 17;104(29):11939-44. Epub 2007 Jul 3. PMID:17609377<ref>PMID:17609377</ref>
-	~~[[http://www.uniprot.org/uniprot/ATRX_HUMAN ATRX_HUMAN]] Defects~~ in ATRX ~~are the cause of alpha~~-~~thalassemia mental retardation syndrome X~~-~~linked~~ (~~ATRX~~) ~~[MIM:[http://omim.org/entry/301040 301040]]. ATR~~-X is an X-linked disorder comprising severe psychomotor retardation, facial dysmorphism, urogenital abnormalities, and alpha-thalassemia. An essential phenotypic trait are hemoglobin H erythrocyte inclusions.<ref>PMID:8968741</ref><ref>PMID:7697714</ref><ref>PMID:9043863</ref><ref>PMID:9326931</ref><ref>PMID:10660327</ref><ref>PMID:10417298</ref><ref>PMID:10204841</ref><ref>PMID:10995512</ref><ref>PMID:12116232</ref><ref>PMID:16955409</ref> Defects in ATRX ~~are the cause of mental retardation syndromic X-linked with hypotonic facies syndrome type 1 (MRXSHF1) [MIM:[http://omim~~.~~org/entry/309580 309580]]; also called Carpenter-Waziri syndrome (CWS)~~, ~~Juberg-Marsidi syndrome (JMS)~~, ~~Smith-Fineman-Myers syndrome type 1 (SFM1). Clinical features include severe mental retardation~~, ~~dysmorphic facies~~, ~~and a highly skewed X-inactivation pattern in carrier women. Other more variable features include hypogonadism~~, ~~deafness~~, ~~renal anomalies~~, ~~and mild skeletal defects~~.<ref>PMID:10751095</ref><ref>PMID:8630485</ref><ref>PMID:10398237</ref><ref>PMID:11050622</ref><ref>PMID:16222662</ref><ref>PMID:15565397</ref> Defects in ATRX are a cause of alpha-thalassemia myelodysplasia syndrome (~~ATMDS~~) ~~[MIM~~:~~[http://omim~~.~~org/entry/300448 300448]]. In this disorder, alpha-thalassemia occurs as an acquired abnormality in association with a multilineage myelodysplasia~~.<ref>PMID:~~12858175~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www.uniprot.org/uniprot/ATRX_HUMAN ATRX_HUMAN]] Could be~~ a ~~global transcriptional regulator~~. ~~Modifies gene expression by affecting chromatin~~. ~~May be involved in brain development and facial morphogenesis~~.	+	</div>
-		+
-	~~==About this Structure==~~	+
-	~~[[2ld1]] is a 1 chain structure with sequence from [http:~~/~~/en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LD1 OCA].~~	+

	==See Also==		==See Also==
	*[[Helicase\|Helicase]]		*[[Helicase\|Helicase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:017609377</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: DNA helicase]]		[[Category: DNA helicase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Neuhaus, D.]]	+	[[Category: Neuhaus, D]]
-	[[Category: Yang, J.]]	+	[[Category: Yang, J]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Metal binding protein]]		[[Category: Metal binding protein]]

OCA at 05:43, 25 March 2013

OCA — Mon, 25 Mar 2013 05:43:38 GMT

←Older revision		Revision as of 05:43, 25 March 2013
Line 1:		Line 1:
-	[[Image:2ld1.png\|left\|200px]]
-
	{{STRUCTURE_2ld1\| PDB=2ld1 \| SCENE= }}		{{STRUCTURE_2ld1\| PDB=2ld1 \| SCENE= }}
-
	===Structures and chemical shift assignments for the ADD domain of the ATRX protein===		===Structures and chemical shift assignments for the ADD domain of the ATRX protein===
		+	{{ABSTRACT_PUBMED_17609377}}

-	~~{{ABSTRACT_PUBMED_17609377}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/ATRX_HUMAN ATRX_HUMAN]] Defects in ATRX are the cause of alpha-thalassemia mental retardation syndrome X-linked (ATRX) [MIM:[http://omim.org/entry/301040 301040]]. ATR-X is an X-linked disorder comprising severe psychomotor retardation, facial dysmorphism, urogenital abnormalities, and alpha-thalassemia. An essential phenotypic trait are hemoglobin H erythrocyte inclusions.<ref>PMID:8968741</ref><ref>PMID:7697714</ref><ref>PMID:9043863</ref><ref>PMID:9326931</ref><ref>PMID:10660327</ref><ref>PMID:10417298</ref><ref>PMID:10204841</ref><ref>PMID:10995512</ref><ref>PMID:12116232</ref><ref>PMID:16955409</ref> Defects in ATRX are the cause of mental retardation syndromic X-linked with hypotonic facies syndrome type 1 (MRXSHF1) [MIM:[http://omim.org/entry/309580 309580]]; also called Carpenter-Waziri syndrome (CWS), Juberg-Marsidi syndrome (JMS), Smith-Fineman-Myers syndrome type 1 (SFM1). Clinical features include severe mental retardation, dysmorphic facies, and a highly skewed X-inactivation pattern in carrier women. Other more variable features include hypogonadism, deafness, renal anomalies, and mild skeletal defects.<ref>PMID:10751095</ref><ref>PMID:8630485</ref><ref>PMID:10398237</ref><ref>PMID:11050622</ref><ref>PMID:16222662</ref><ref>PMID:15565397</ref> Defects in ATRX are a cause of alpha-thalassemia myelodysplasia syndrome (ATMDS) [MIM:[http://omim.org/entry/300448 300448]]. In this disorder, alpha-thalassemia occurs as an acquired abnormality in association with a multilineage myelodysplasia.<ref>PMID:12858175</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/ATRX_HUMAN ATRX_HUMAN]] Could be a global transcriptional regulator. Modifies gene expression by affecting chromatin. May be involved in brain development and facial morphogenesis.

	==About this Structure==		==About this Structure==
Line 14:		Line 16:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:017609377</ref><references group="xtra"/>	+	<ref group="xtra">PMID:017609377</ref><references group="xtra"/><references/>
	[[Category: DNA helicase]]		[[Category: DNA helicase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 09:09, 20 October 2012

OCA — Sat, 20 Oct 2012 09:09:00 GMT

←Older revision		Revision as of 09:09, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[2ld1]] is a 1 chain structure ~~of [[Helicase]]~~ with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LD1 OCA].	+	[[2ld1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LD1 OCA].

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

OCA at 21:54, 25 July 2012

OCA — Wed, 25 Jul 2012 21:54:24 GMT

←Older revision		Revision as of 21:54, 25 July 2012
Line 1:		Line 1:
-	[[Image:2ld1.~~jpg~~\|left\|200px]]	+	[[Image:2ld1.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2ld1", 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_2ld1\| PDB=2ld1 \| SCENE= }}		{{STRUCTURE_2ld1\| PDB=2ld1 \| SCENE= }}

	===Structures and chemical shift assignments for the ADD domain of the ATRX protein===		===Structures and chemical shift assignments for the ADD domain of the ATRX protein===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_17609377}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 17609377 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_17609377}}		{{ABSTRACT_PUBMED_17609377}}

	==About this Structure==		==About this Structure==
-	[[2ld1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LD1 OCA].	+	[[2ld1]] is a 1 chain structure of [[Helicase]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LD1 OCA].
		+
		+	==See Also==
		+	*[[Helicase\|Helicase]]

	==Reference==		==Reference==
Line 27:		Line 19:
	[[Category: Neuhaus, D.]]		[[Category: Neuhaus, D.]]
	[[Category: Yang, J.]]		[[Category: Yang, J.]]
		+	[[Category: Hydrolase]]
		+	[[Category: Metal binding protein]]

OCA at 05:10, 8 June 2011

OCA — Wed, 08 Jun 2011 05:10:42 GMT

←Older revision		Revision as of 05:10, 8 June 2011
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:2ld1.jpg\|left\|200px]]

-	The ~~entry 2ld1~~ is ~~ON HOLD~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_2ld1", 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_2ld1\| PDB=2ld1 \| SCENE= }}

-	~~Authors: Neuhaus, D., Yang, J.~~	+	===Structures and chemical shift assignments for the ADD domain of the ATRX protein===

-	~~Description: Structures and chemical shift assignments for~~ the ~~ADD domain of~~ the ~~ATRX protein~~	+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_17609377}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 17609377 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_17609377}}
		+
		+	==About this Structure==
		+	[[2ld1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LD1 OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:017609377</ref><references group="xtra"/>
		+	[[Category: DNA helicase]]
		+	[[Category: Homo sapiens]]
		+	[[Category: Neuhaus, D.]]
		+	[[Category: Yang, J.]]