4apt - Revision history

OCA at 11:32, 20 December 2023

2023-12-20T11:32:38Z

← Older revision		Revision as of 11:32, 20 December 2023
Line 3:		Line 3:
	<StructureSection load='4apt' size='340' side='right'caption='[[4apt]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='4apt' size='340' side='right'caption='[[4apt]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4apt]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4APT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4APT FirstGlance]. <br>		<table><tr><td colspan='2'>[[4apt]] is a 4 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=4APT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4APT FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2.5Å</td></tr>
	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[1oa8\|1oa8]], [[4aqp\|4aqp]]~~</~~div~~></td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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=4apt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4apt OCA], [https://pdbe.org/4apt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4apt RCSB], [https://www.ebi.ac.uk/pdbsum/4apt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4apt 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=4apt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4apt OCA], [https://pdbe.org/4apt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4apt RCSB], [https://www.ebi.ac.uk/pdbsum/4apt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4apt ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[https://www.uniprot.org/uniprot/ATX1_HUMAN ATX1_HUMAN]] Spinocerebellar ataxia type 1. Defects in ATXN1 are the cause of spinocerebellar ataxia type 1 (SCA1) [MIM:[https://omim.org/entry/164400 164400]]; also known as olivopontocerebellar atrophy I (OPCA I or OPCA1). Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to cerebellum degeneration with variable involvement of the brainstem and spinal cord. SCA1 belongs to the autosomal dominant cerebellar ataxias type I (ADCA I) which are characterized by cerebellar ataxia in combination with additional clinical features like optic atrophy, ophthalmoplegia, bulbar and extrapyramidal signs, peripheral neuropathy and dementia. SCA1 is caused by expansion of a CAG repeat in the coding region of ATXN1. Longer expansions result in earlier onset and more severe clinical manifestations of the disease.<ref>PMID:7951322</ref> <ref>PMID:8634720</ref>		[https://www.uniprot.org/uniprot/ATX1_HUMAN ATX1_HUMAN] Spinocerebellar ataxia type 1. Defects in ATXN1 are the cause of spinocerebellar ataxia type 1 (SCA1) [MIM:[https://omim.org/entry/164400 164400]; also known as olivopontocerebellar atrophy I (OPCA I or OPCA1). Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to cerebellum degeneration with variable involvement of the brainstem and spinal cord. SCA1 belongs to the autosomal dominant cerebellar ataxias type I (ADCA I) which are characterized by cerebellar ataxia in combination with additional clinical features like optic atrophy, ophthalmoplegia, bulbar and extrapyramidal signs, peripheral neuropathy and dementia. SCA1 is caused by expansion of a CAG repeat in the coding region of ATXN1. Longer expansions result in earlier onset and more severe clinical manifestations of the disease.<ref>PMID:7951322</ref> <ref>PMID:8634720</ref>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/ATX1_HUMAN ATX1_HUMAN]] Chromatin-binding factor that repress Notch signaling in the absence of Notch intracellular domain by acting as a CBF1 corepressor. Binds to the HEY promoter and might assist, along with NCOR2, RBPJ-mediated repression. Binds RNA in vitro. May be involved in RNA metabolism. The expansion of the polyglutamine tract may alter this function.<ref>PMID:21475249</ref>		[https://www.uniprot.org/uniprot/ATX1_HUMAN ATX1_HUMAN] Chromatin-binding factor that repress Notch signaling in the absence of Notch intracellular domain by acting as a CBF1 corepressor. Binds to the HEY promoter and might assist, along with NCOR2, RBPJ-mediated repression. Binds RNA in vitro. May be involved in RNA metabolism. The expansion of the polyglutamine tract may alter this function.<ref>PMID:21475249</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Human~~]]		[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Chen~~, Y W]]~~		[[Category: Chen YW]]
	~~[[Category: Chiara, C de~~]]		[[Category: Pastore A]]
	[[Category: Pastore, A]]		[[Category: Rees M]]
	[[Category: Rees, M]]		[[Category: De Chiara C]]
	[[Category: ~~Dimerization]]~~
	~~[[Category: High mobility group homology]]~~
	~~[[Category: Hmg]]~~
	~~[[Category: Ob-fold]]~~
	~~[[Category: Rna binding]]~~
	~~[[Category: Rna binding protein~~]]

OCA at 05:42, 25 August 2022

2022-08-25T05:42:07Z

← Older revision		Revision as of 05:42, 25 August 2022
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	<StructureSection load='4apt' size='340' side='right'caption='[[4apt]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='4apt' size='340' side='right'caption='[[4apt]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4apt]] is a 4 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=4APT OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4APT FirstGlance]. <br>		<table><tr><td colspan='2'>[[4apt]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4APT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4APT FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1oa8\|1oa8]], [[4aqp\|4aqp]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1oa8\|1oa8]], [[4aqp\|4aqp]]</div></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=4apt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4apt OCA], [~~http~~://pdbe.org/4apt PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4apt RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4apt PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4apt 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=4apt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4apt OCA], [https://pdbe.org/4apt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4apt RCSB], [https://www.ebi.ac.uk/pdbsum/4apt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4apt ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[~~http~~://www.uniprot.org/uniprot/ATX1_HUMAN ATX1_HUMAN]] Spinocerebellar ataxia type 1. Defects in ATXN1 are the cause of spinocerebellar ataxia type 1 (SCA1) [MIM:[~~http~~://omim.org/entry/164400 164400]]; also known as olivopontocerebellar atrophy I (OPCA I or OPCA1). Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to cerebellum degeneration with variable involvement of the brainstem and spinal cord. SCA1 belongs to the autosomal dominant cerebellar ataxias type I (ADCA I) which are characterized by cerebellar ataxia in combination with additional clinical features like optic atrophy, ophthalmoplegia, bulbar and extrapyramidal signs, peripheral neuropathy and dementia. SCA1 is caused by expansion of a CAG repeat in the coding region of ATXN1. Longer expansions result in earlier onset and more severe clinical manifestations of the disease.<ref>PMID:7951322</ref> <ref>PMID:8634720</ref>		[[https://www.uniprot.org/uniprot/ATX1_HUMAN ATX1_HUMAN]] Spinocerebellar ataxia type 1. Defects in ATXN1 are the cause of spinocerebellar ataxia type 1 (SCA1) [MIM:[https://omim.org/entry/164400 164400]]; also known as olivopontocerebellar atrophy I (OPCA I or OPCA1). Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to cerebellum degeneration with variable involvement of the brainstem and spinal cord. SCA1 belongs to the autosomal dominant cerebellar ataxias type I (ADCA I) which are characterized by cerebellar ataxia in combination with additional clinical features like optic atrophy, ophthalmoplegia, bulbar and extrapyramidal signs, peripheral neuropathy and dementia. SCA1 is caused by expansion of a CAG repeat in the coding region of ATXN1. Longer expansions result in earlier onset and more severe clinical manifestations of the disease.<ref>PMID:7951322</ref> <ref>PMID:8634720</ref>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/ATX1_HUMAN ATX1_HUMAN]] Chromatin-binding factor that repress Notch signaling in the absence of Notch intracellular domain by acting as a CBF1 corepressor. Binds to the HEY promoter and might assist, along with NCOR2, RBPJ-mediated repression. Binds RNA in vitro. May be involved in RNA metabolism. The expansion of the polyglutamine tract may alter this function.<ref>PMID:21475249</ref>		[[https://www.uniprot.org/uniprot/ATX1_HUMAN ATX1_HUMAN]] Chromatin-binding factor that repress Notch signaling in the absence of Notch intracellular domain by acting as a CBF1 corepressor. Binds to the HEY promoter and might assist, along with NCOR2, RBPJ-mediated repression. Binds RNA in vitro. May be involved in RNA metabolism. The expansion of the polyglutamine tract may alter this function.<ref>PMID:21475249</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 26:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
			[[Category: Large Structures]]
	[[Category: Chen, Y W]]		[[Category: Chen, Y W]]
	[[Category: Chiara, C de]]		[[Category: Chiara, C de]]

OCA at 09:44, 6 March 2019

2019-03-06T09:44:20Z

← Older revision		Revision as of 09:44, 6 March 2019
Line 1:		Line 1:

	==The structure of the AXH domain of ataxin-1.==		==The structure of the AXH domain of ataxin-1.==
	<StructureSection load='4apt' size='340' side='right' caption='[[4apt]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='4apt' size='340' side='right'caption='[[4apt]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4apt]] is a 4 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=4APT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4APT FirstGlance]. <br>		<table><tr><td colspan='2'>[[4apt]] is a 4 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=4APT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4APT FirstGlance]. <br>

OCA at 12:02, 4 August 2016

2016-08-04T12:02:42Z

← Older revision		Revision as of 12:02, 4 August 2016
Line 1:		Line 1:

	==The structure of the AXH domain of ataxin-1.==		==The structure of the AXH domain of ataxin-1.==
	<StructureSection load='4apt' size='340' side='right' caption='[[4apt]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='4apt' size='340' side='right' caption='[[4apt]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4apt]] is a 4 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=4APT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4APT FirstGlance]. <br>		<table><tr><td colspan='2'>[[4apt]] is a 4 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=4APT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4APT FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1oa8\|1oa8]], [[4aqp\|4aqp]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1oa8\|1oa8]], [[4aqp\|4aqp]]</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=4apt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4apt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4apt RCSB], [http://www.ebi.ac.uk/pdbsum/4apt 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=4apt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4apt OCA], [http://pdbe.org/4apt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4apt RCSB], [http://www.ebi.ac.uk/pdbsum/4apt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4apt ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 19:		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 4apt" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Homo sapiens~~]]		[[Category: Human]]
	[[Category: Chen, Y W]]		[[Category: Chen, Y W]]
	[[Category: Chiara, C de]]		[[Category: Chiara, C de]]

OCA at 10:10, 21 December 2014

2014-12-21T10:10:47Z

← Older revision		Revision as of 10:10, 21 December 2014
Line 1:		Line 1:
	~~{{STRUCTURE_4apt\| PDB=4apt \| SCENE= }}~~		==The structure of the AXH domain of ataxin-1.==
	===The structure of the AXH domain of ataxin-1.===		<StructureSection load='4apt' size='340' side='right' caption='[[4apt]], [[Resolution\|resolution]] 2.50Å' scene=''>
	~~{{ABSTRACT_PUBMED_23528090}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[4apt]] is a 4 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=4APT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4APT FirstGlance]. <br>
	==Disease==		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
			<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1oa8\|1oa8]], [[4aqp\|4aqp]]</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=4apt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4apt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4apt RCSB], [http://www.ebi.ac.uk/pdbsum/4apt PDBsum]</span></td></tr>
			</table>
			== Disease ==
	[[http://www.uniprot.org/uniprot/ATX1_HUMAN ATX1_HUMAN]] Spinocerebellar ataxia type 1. Defects in ATXN1 are the cause of spinocerebellar ataxia type 1 (SCA1) [MIM:[http://omim.org/entry/164400 164400]]; also known as olivopontocerebellar atrophy I (OPCA I or OPCA1). Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to cerebellum degeneration with variable involvement of the brainstem and spinal cord. SCA1 belongs to the autosomal dominant cerebellar ataxias type I (ADCA I) which are characterized by cerebellar ataxia in combination with additional clinical features like optic atrophy, ophthalmoplegia, bulbar and extrapyramidal signs, peripheral neuropathy and dementia. SCA1 is caused by expansion of a CAG repeat in the coding region of ATXN1. Longer expansions result in earlier onset and more severe clinical manifestations of the disease.<ref>PMID:7951322</ref> <ref>PMID:8634720</ref>		[[http://www.uniprot.org/uniprot/ATX1_HUMAN ATX1_HUMAN]] Spinocerebellar ataxia type 1. Defects in ATXN1 are the cause of spinocerebellar ataxia type 1 (SCA1) [MIM:[http://omim.org/entry/164400 164400]]; also known as olivopontocerebellar atrophy I (OPCA I or OPCA1). Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to cerebellum degeneration with variable involvement of the brainstem and spinal cord. SCA1 belongs to the autosomal dominant cerebellar ataxias type I (ADCA I) which are characterized by cerebellar ataxia in combination with additional clinical features like optic atrophy, ophthalmoplegia, bulbar and extrapyramidal signs, peripheral neuropathy and dementia. SCA1 is caused by expansion of a CAG repeat in the coding region of ATXN1. Longer expansions result in earlier onset and more severe clinical manifestations of the disease.<ref>PMID:7951322</ref> <ref>PMID:8634720</ref>
			== Function ==
	==Function==
	[[http://www.uniprot.org/uniprot/ATX1_HUMAN ATX1_HUMAN]] Chromatin-binding factor that repress Notch signaling in the absence of Notch intracellular domain by acting as a CBF1 corepressor. Binds to the HEY promoter and might assist, along with NCOR2, RBPJ-mediated repression. Binds RNA in vitro. May be involved in RNA metabolism. The expansion of the polyglutamine tract may alter this function.<ref>PMID:21475249</ref>		[[http://www.uniprot.org/uniprot/ATX1_HUMAN ATX1_HUMAN]] Chromatin-binding factor that repress Notch signaling in the absence of Notch intracellular domain by acting as a CBF1 corepressor. Binds to the HEY promoter and might assist, along with NCOR2, RBPJ-mediated repression. Binds RNA in vitro. May be involved in RNA metabolism. The expansion of the polyglutamine tract may alter this function.<ref>PMID:21475249</ref>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Ataxin-1 is a human protein responsible for spinocerebellar ataxia type 1, a hereditary disease associated with protein aggregation and misfolding. Essential for ataxin-1 aggregation is the anomalous expansion of a polyglutamine tract near the protein N-terminus, but the sequence-wise distant AXH domain modulates and contributes to the process. The AXH domain is also involved in the nonpathologic functions of the protein, including a variety of intermolecular interactions with other cellular partners. The domain forms a globular dimer in solution and displays a dimer of dimers arrangement in the crystal asymmetric unit. Here, we have characterized the domain further by studying its behavior in the crystal and in solution. We solved two new structures of the domain crystallized under different conditions that confirm an inherent plasticity of the AXH fold. In solution, the domain is present as a complex equilibrium mixture of monomeric, dimeric, and higher molecular weight species. This behavior, together with the tendency of the AXH fold to be trapped in local conformations, and the multiplicity of protomer interfaces, makes the AXH domain an unusual example of a chameleon protein whose properties bear potential relevance for the aggregation properties of ataxin-1 and thus for disease.

	~~==About this Structure==~~		Self-Assembly and Conformational Heterogeneity of the AXH Domain of Ataxin-1: An Unusual Example of a Chameleon Fold.,de Chiara C, Rees M, Menon RP, Pauwels K, Lawrence C, Konarev PV, Svergun DI, Martin SR, Chen YW, Pastore A Biophys J. 2013 Mar 19;104(6):1304-13. doi: 10.1016/j.bpj.2013.01.048. Epub 2013 , Mar 19. PMID:23528090<ref>PMID:23528090</ref>
	~~[[4apt]] is~~ a ~~4 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=4APT OCA].~~

	==~~Reference~~==		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	~~<ref group="xtra">PMID:014583607</ref>~~<references ~~group="xtra"~~/><~~references~~/>		</div>
			== References ==
			<references/>
			__TOC__
			</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Chen, Y W.]]		[[Category: Chen, Y W]]
	[[Category: Chiara, C de.]]		[[Category: Chiara, C de]]
	[[Category: Pastore, A.]]		[[Category: Pastore, A]]
	[[Category: Rees, M.]]		[[Category: Rees, M]]
	[[Category: Dimerization]]		[[Category: Dimerization]]
	[[Category: High mobility group homology]]		[[Category: High mobility group homology]]

OCA at 19:32, 17 April 2013

2013-04-17T19:32:16Z

← Older revision		Revision as of 19:32, 17 April 2013
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	{{STRUCTURE_4apt\| PDB=4apt \| SCENE= }}		{{STRUCTURE_4apt\| PDB=4apt \| SCENE= }}
	===The structure of the AXH domain of ataxin-1.===		===The structure of the AXH domain of ataxin-1.===
	{{~~ABSTRACT_PUBMED_14583607~~}}		{{ABSTRACT_PUBMED_23528090}}

	==Disease==		==Disease==
	[[http://www.uniprot.org/uniprot/ATX1_HUMAN ATX1_HUMAN]] Spinocerebellar ataxia type 1. Defects in ATXN1 are the cause of spinocerebellar ataxia type 1 (SCA1) [MIM:[http://omim.org/entry/164400 164400]]; also known as olivopontocerebellar atrophy I (OPCA I or OPCA1). Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to cerebellum degeneration with variable involvement of the brainstem and spinal cord. SCA1 belongs to the autosomal dominant cerebellar ataxias type I (ADCA I) which are characterized by cerebellar ataxia in combination with additional clinical features like optic atrophy, ophthalmoplegia, bulbar and extrapyramidal signs, peripheral neuropathy and dementia. SCA1 is caused by expansion of a CAG repeat in the coding region of ATXN1. Longer expansions result in earlier onset and more severe clinical manifestations of the disease.<ref>PMID:7951322</ref><ref>PMID:8634720</ref>		[[http://www.uniprot.org/uniprot/ATX1_HUMAN ATX1_HUMAN]] Spinocerebellar ataxia type 1. Defects in ATXN1 are the cause of spinocerebellar ataxia type 1 (SCA1) [MIM:[http://omim.org/entry/164400 164400]]; also known as olivopontocerebellar atrophy I (OPCA I or OPCA1). Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to cerebellum degeneration with variable involvement of the brainstem and spinal cord. SCA1 belongs to the autosomal dominant cerebellar ataxias type I (ADCA I) which are characterized by cerebellar ataxia in combination with additional clinical features like optic atrophy, ophthalmoplegia, bulbar and extrapyramidal signs, peripheral neuropathy and dementia. SCA1 is caused by expansion of a CAG repeat in the coding region of ATXN1. Longer expansions result in earlier onset and more severe clinical manifestations of the disease.<ref>PMID:7951322</ref> <ref>PMID:8634720</ref>

	==Function==		==Function==
	[[http://www.uniprot.org/uniprot/ATX1_HUMAN ATX1_HUMAN]] Chromatin-binding factor that repress Notch signaling in the absence of Notch intracellular domain by acting as a CBF1 corepressor. Binds to the HEY promoter and might assist, along with NCOR2, RBPJ-mediated repression. Binds RNA in vitro. May be involved in RNA metabolism. The expansion of the polyglutamine tract may alter this function.<ref>PMID:21475249</ref>		[[http://www.uniprot.org/uniprot/ATX1_HUMAN ATX1_HUMAN]] Chromatin-binding factor that repress Notch signaling in the absence of Notch intracellular domain by acting as a CBF1 corepressor. Binds to the HEY promoter and might assist, along with NCOR2, RBPJ-mediated repression. Binds RNA in vitro. May be involved in RNA metabolism. The expansion of the polyglutamine tract may alter this function.<ref>PMID:21475249</ref>

	==About this Structure==		==About this Structure==
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	==Reference==		==Reference==
	<ref group="xtra">PMID:014583607~~</ref><ref group="xtra">PMID:012965213~~</ref><references group="xtra"/><references/>		<ref group="xtra">PMID:014583607</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Chen, Y W.]]		[[Category: Chen, Y W.]]

OCA at 08:55, 27 March 2013

2013-03-27T08:55:09Z

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+{{STRUCTURE_4apt|  PDB=4apt  |  SCENE=  }}
-The entry 4apt is ON HOLD  until Paper Publication
+==Disease==
-Authors: Rees, M., Chen, Y.W., de Chira, C., Pastore, A.
+==Function==
-Description: The structure of the AXH domain of ataxin-1.
+==About this Structure==

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

2012-04-11T06:35:20Z

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

← Older revision	Revision as of 06:35, 11 April 2012
(No difference)

OCA: New page: '''Unreleased structure''' The entry 4apt is ON HOLD until Paper Publication Authors: Rees, M., Chen, Y.W., de Chira, C., Pastore, A. Description: The structure of the AXH domain of at...

2012-04-11T06:35:19Z

New page: '''Unreleased structure''' The entry 4apt is ON HOLD until Paper Publication Authors: Rees, M., Chen, Y.W., de Chira, C., Pastore, A. Description: The structure of the AXH domain of at...

New page

'''Unreleased structure'''

The entry 4apt is ON HOLD until Paper Publication

Authors: Rees, M., Chen, Y.W., de Chira, C., Pastore, A.

Description: The structure of the AXH domain of ataxin-1.