1a7i - Revision history

OCA at 08:11, 22 May 2024

2024-05-22T08:11:52Z

←Older revision		Revision as of 08:11, 22 May 2024
Line 20:		Line 20:
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1a7i ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1a7i ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Members of the cysteine and glycine-rich protein (CRP) family (CRP1, CRP2, and CRP3) contain two zinc-binding LIM domains, LIM1 and LIM2, and are implicated in diverse cellular processes linked to differentiation, growth control and pathogenesis. The solution structure of an 81-amino acid recombinant peptide encompassing the amino-terminal LIM1 domain of quail CRP2 has been determined by 2D and 3D homo- and heteronuclear NMR spectroscopy. The LIM1 domain consists of two zinc binding sites of the CCHC and the CCCC type, respectively, which both contain two orthogonally arranged antiparallel beta-sheets and which are packed together by a hydrophobic core composed of residues from the zinc finger loop regions. The CCCC zinc finger is followed by a short alpha-helical stretch. The structural analysis revealed that the global fold of LIM1 closely resembles the recently determined solution structures of the carboxyl-terminal LIM2 domains of quail CRP2 and chicken CRP1, and that LIM1 and LIM2 are independently folded structural and presumably functional domains of CRP proteins. To explore the dynamical properties of CRP proteins, we have used 15N relaxation values (T1, T2, and nuclear Overhauser effect (NOE) to describe the dynamical behavior of a LIM domain. A model-free analysis revealed local variations in mobility along the backbone of the quail CRP2 LIM1 motif. Slow motions are evident in turn regions located between the various antiparallel beta-sheets or between their strands. By use of an extended motional model, fast backbone motions were detected for backbone amide NH groups of hydrophobic residues located in the core region of the LIM1 domain. These findings point to a flexible hydrophobic core in the LIM1 domain allowing residual relative mobility of the two zinc fingers, which might be important to optimize the LIM1 interface for interaction with its physiological target molecule(s) and to compensate enthalpically for the entropy loss upon binding.
		+
		+	Structure and intramodular dynamics of the amino-terminal LIM domain from quail cysteine- and glycine-rich protein CRP2.,Kontaxis G, Konrat R, Krautler B, Weiskirchen R, Bister K Biochemistry. 1998 May 19;37(20):7127-34. PMID:9585524<ref>PMID:9585524</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 1a7i" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 15:21, 13 March 2024

2024-03-13T15:21:55Z

←Older revision		Revision as of 15:21, 13 March 2024
Line 1:		Line 1:

	==AMINO-TERMINAL LIM DOMAIN FROM QUAIL CYSTEINE AND GLYCINE-RICH PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE==		==AMINO-TERMINAL LIM DOMAIN FROM QUAIL CYSTEINE AND GLYCINE-RICH PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE==
-	<StructureSection load='1a7i' size='340' side='right'caption='[[1a7i~~]], [[NMR_Ensembles_of_Models \| 1 NMR models~~]]' scene=''>	+	<StructureSection load='1a7i' size='340' side='right'caption='[[1a7i]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1a7i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Cotja Cotja~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A7I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A7I FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1a7i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Coturnix_japonica Coturnix japonica]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A7I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A7I 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='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~CSRP2 ([https~~:/~~/www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=93934 COTJA])~~</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=1a7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a7i OCA], [https://pdbe.org/1a7i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a7i RCSB], [https://www.ebi.ac.uk/pdbsum/1a7i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a7i 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=1a7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a7i OCA], [https://pdbe.org/1a7i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a7i RCSB], [https://www.ebi.ac.uk/pdbsum/1a7i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a7i ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/CSRP2_COTJA CSRP2_COTJA]] Interacts with zyxin. May be a component of a signal transduction pathway that mediates adhesion-stimulated changes in gene expression. Totally down-regulated in transformed cells.	+	[https://www.uniprot.org/uniprot/CSRP2_COTJA CSRP2_COTJA] Interacts with zyxin. May be a component of a signal transduction pathway that mediates adhesion-stimulated changes in gene expression. Totally down-regulated in transformed cells.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 20:		Line 20:
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1a7i ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1a7i ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Members of the cysteine and glycine-rich protein (CRP) family (CRP1, CRP2, and CRP3) contain two zinc-binding LIM domains, LIM1 and LIM2, and are implicated in diverse cellular processes linked to differentiation, growth control and pathogenesis. The solution structure of an 81-amino acid recombinant peptide encompassing the amino-terminal LIM1 domain of quail CRP2 has been determined by 2D and 3D homo- and heteronuclear NMR spectroscopy. The LIM1 domain consists of two zinc binding sites of the CCHC and the CCCC type, respectively, which both contain two orthogonally arranged antiparallel beta-sheets and which are packed together by a hydrophobic core composed of residues from the zinc finger loop regions. The CCCC zinc finger is followed by a short alpha-helical stretch. The structural analysis revealed that the global fold of LIM1 closely resembles the recently determined solution structures of the carboxyl-terminal LIM2 domains of quail CRP2 and chicken CRP1, and that LIM1 and LIM2 are independently folded structural and presumably functional domains of CRP proteins. To explore the dynamical properties of CRP proteins, we have used 15N relaxation values (T1, T2, and nuclear Overhauser effect (NOE) to describe the dynamical behavior of a LIM domain. A model-free analysis revealed local variations in mobility along the backbone of the quail CRP2 LIM1 motif. Slow motions are evident in turn regions located between the various antiparallel beta-sheets or between their strands. By use of an extended motional model, fast backbone motions were detected for backbone amide NH groups of hydrophobic residues located in the core region of the LIM1 domain. These findings point to a flexible hydrophobic core in the LIM1 domain allowing residual relative mobility of the two zinc fingers, which might be important to optimize the LIM1 interface for interaction with its physiological target molecule(s) and to compensate enthalpically for the entropy loss upon binding.
-
-	Structure and intramodular dynamics of the amino-terminal LIM domain from quail cysteine- and glycine-rich protein CRP2.,Kontaxis G, Konrat R, Krautler B, Weiskirchen R, Bister K Biochemistry. 1998 May 19;37(20):7127-34. PMID:9585524<ref>PMID:9585524</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1a7i" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Cotja~~]]	+	[[Category: Coturnix japonica]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bister, K]]	+	[[Category: Bister K]]
-	[[Category: Konrat, R]]	+	[[Category: Konrat R]]
-	[[Category: Kontaxis, G]]	+	[[Category: Kontaxis G]]
-	[[Category: Kraeutler, B]]	+	[[Category: Kraeutler B]]
-	[[Category: Weiskirchen, R]]	+	[[Category: Weiskirchen R]]
-	~~[[Category: Lim domain containing protein]]~~	+
-	~~[[Category: Metal-binding protein]]~~	+
-	~~[[Category: Zinc finger~~]]	+

OCA at 10:21, 16 February 2022

2022-02-16T10:21:28Z

←Older revision		Revision as of 10:21, 16 February 2022
Line 3:		Line 3:
	<StructureSection load='1a7i' size='340' side='right'caption='[[1a7i]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1a7i' size='340' side='right'caption='[[1a7i]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1a7i]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A7I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A7I FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1a7i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cotja Cotja]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A7I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A7I 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">CSRP2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=93934 COTJA])</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=1a7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a7i OCA], [https://pdbe.org/1a7i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a7i RCSB], [https://www.ebi.ac.uk/pdbsum/1a7i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a7i 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=1a7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a7i OCA], [https://pdbe.org/1a7i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a7i RCSB], [https://www.ebi.ac.uk/pdbsum/1a7i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a7i ProSAT]</span></td></tr>
	</table>		</table>
Line 32:		Line 33:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Cotja]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Bister, K]]		[[Category: Bister, K]]

OCA at 10:17, 17 February 2021

2021-02-17T10:17:36Z

←Older revision		Revision as of 10:17, 17 February 2021
Line 3:		Line 3:
	<StructureSection load='1a7i' size='340' side='right'caption='[[1a7i]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1a7i' size='340' side='right'caption='[[1a7i]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1a7i]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A7I OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1A7I FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1a7i]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A7I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A7I 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='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=1a7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a7i OCA], [~~http~~://pdbe.org/1a7i PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1a7i RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1a7i PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1a7i 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=1a7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a7i OCA], [https://pdbe.org/1a7i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a7i RCSB], [https://www.ebi.ac.uk/pdbsum/1a7i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a7i ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/CSRP2_COTJA CSRP2_COTJA]] Interacts with zyxin. May be a component of a signal transduction pathway that mediates adhesion-stimulated changes in gene expression. Totally down-regulated in transformed cells.	+	[[https://www.uniprot.org/uniprot/CSRP2_COTJA CSRP2_COTJA]] Interacts with zyxin. May be a component of a signal transduction pathway that mediates adhesion-stimulated changes in gene expression. Totally down-regulated in transformed cells.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 14:38, 10 May 2019

2019-05-10T14:38:01Z

←Older revision		Revision as of 14:38, 10 May 2019
Line 1:		Line 1:

	==AMINO-TERMINAL LIM DOMAIN FROM QUAIL CYSTEINE AND GLYCINE-RICH PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE==		==AMINO-TERMINAL LIM DOMAIN FROM QUAIL CYSTEINE AND GLYCINE-RICH PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE==
-	<StructureSection load='1a7i' size='340' side='right' caption='[[1a7i]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>	+	<StructureSection load='1a7i' size='340' side='right'caption='[[1a7i]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1a7i]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A7I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A7I FirstGlance]. <br>		<table><tr><td colspan='2'>[[1a7i]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A7I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A7I FirstGlance]. <br>
Line 13:		Line 13:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a7/1a7i_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a7/1a7i_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 32:		Line 32:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Bister, K]]		[[Category: Bister, K]]
	[[Category: Konrat, R]]		[[Category: Konrat, R]]

OCA at 09:08, 9 August 2017

2017-08-09T09:08:48Z

←Older revision		Revision as of 09:08, 9 August 2017
Line 1:		Line 1:
		+
	==AMINO-TERMINAL LIM DOMAIN FROM QUAIL CYSTEINE AND GLYCINE-RICH PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE==		==AMINO-TERMINAL LIM DOMAIN FROM QUAIL CYSTEINE AND GLYCINE-RICH PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE==
	<StructureSection load='1a7i' size='340' side='right' caption='[[1a7i]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1a7i' size='340' side='right' caption='[[1a7i]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1a7i]] is a 1 chain structure ~~with sequence from [http://en.wikipedia.org/wiki/Cotja Cotja]~~. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A7I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A7I FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1a7i]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A7I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A7I 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">CSRP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=93934 COTJA])</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=1a7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a7i OCA], [http://pdbe.org/1a7i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1a7i RCSB], [http://www.ebi.ac.uk/pdbsum/1a7i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1a7i ProSAT]</span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a7i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a7i RCSB], [http://www.ebi.ac.uk/pdbsum/1a7i PDBsum]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 17:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1a7i ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 32:		Line 32:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Cotja]]
	[[Category: Bister, K]]		[[Category: Bister, K]]
	[[Category: Konrat, R]]		[[Category: Konrat, R]]

OCA at 15:37, 9 September 2015

2015-09-09T15:37:02Z

←Older revision		Revision as of 15:37, 9 September 2015
Line 2:		Line 2:
	<StructureSection load='1a7i' size='340' side='right' caption='[[1a7i]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1a7i' size='340' side='right' caption='[[1a7i]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1a7i]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Coturnix_japonica Coturnix japonica~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A7I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A7I FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1a7i]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cotja Cotja]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A7I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A7I 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">CSRP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=93934 ~~Coturnix japonica~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CSRP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=93934 COTJA])</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=1a7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a7i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a7i RCSB], [http://www.ebi.ac.uk/pdbsum/1a7i 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=1a7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a7i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a7i RCSB], [http://www.ebi.ac.uk/pdbsum/1a7i PDBsum]</span></td></tr>
	</table>		</table>
Line 27:		Line 27:
	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 1a7i" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Coturnix japonica~~]]	+	[[Category: Cotja]]
	[[Category: Bister, K]]		[[Category: Bister, K]]
	[[Category: Konrat, R]]		[[Category: Konrat, R]]

OCA at 17:18, 25 December 2014

2014-12-25T17:18:50Z

←Older revision		Revision as of 17:18, 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=1a7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a7i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a7i RCSB], [http://www.ebi.ac.uk/pdbsum/1a7i 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=1a7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a7i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a7i RCSB], [http://www.ebi.ac.uk/pdbsum/1a7i PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CSRP2_COTJA CSRP2_COTJA]] Interacts with zyxin. May be a component of a signal transduction pathway that mediates adhesion-stimulated changes in gene expression. Totally down-regulated in transformed cells.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 08:58, 22 December 2014

2014-12-22T08:58:39Z

←Older revision		Revision as of 08:58, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1a7i]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Coturnix_japonica Coturnix japonica]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A7I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A7I FirstGlance]. <br>		<table><tr><td colspan='2'>[[1a7i]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Coturnix_japonica Coturnix japonica]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A7I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A7I FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><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><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CSRP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=93934 Coturnix japonica])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CSRP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=93934 Coturnix japonica])</td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a7i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a7i RCSB], [http://www.ebi.ac.uk/pdbsum/1a7i 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=1a7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a7i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a7i RCSB], [http://www.ebi.ac.uk/pdbsum/1a7i PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 30:		Line 30:
	</StructureSection>		</StructureSection>
	[[Category: Coturnix japonica]]		[[Category: Coturnix japonica]]
-	[[Category: Bister, K.]]	+	[[Category: Bister, K]]
-	[[Category: Konrat, R.]]	+	[[Category: Konrat, R]]
-	[[Category: Kontaxis, G.]]	+	[[Category: Kontaxis, G]]
-	[[Category: Kraeutler, B.]]	+	[[Category: Kraeutler, B]]
-	[[Category: Weiskirchen, R.]]	+	[[Category: Weiskirchen, R]]
	[[Category: Lim domain containing protein]]		[[Category: Lim domain containing protein]]
	[[Category: Metal-binding protein]]		[[Category: Metal-binding protein]]
	[[Category: Zinc finger]]		[[Category: Zinc finger]]

OCA at 08:24, 23 July 2014

2014-07-23T08:24:02Z

←Older revision		Revision as of 08:24, 23 July 2014
Line 1:		Line 1:
-	[[~~Image:~~1a7i.~~png~~\|~~left~~\|200px]]	+	==AMINO-TERMINAL LIM DOMAIN FROM QUAIL CYSTEINE AND GLYCINE-RICH PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE==
		+	<StructureSection load='1a7i' size='340' side='right' caption='[[1a7i]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1a7i]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Coturnix_japonica Coturnix japonica]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A7I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A7I FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CSRP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=93934 Coturnix japonica])</td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a7i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a7i RCSB], [http://www.ebi.ac.uk/pdbsum/1a7i PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a7/1a7i_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Members of the cysteine and glycine-rich protein (CRP) family (CRP1, CRP2, and CRP3) contain two zinc-binding LIM domains, LIM1 and LIM2, and are implicated in diverse cellular processes linked to differentiation, growth control and pathogenesis. The solution structure of an 81-amino acid recombinant peptide encompassing the amino-terminal LIM1 domain of quail CRP2 has been determined by 2D and 3D homo- and heteronuclear NMR spectroscopy. The LIM1 domain consists of two zinc binding sites of the CCHC and the CCCC type, respectively, which both contain two orthogonally arranged antiparallel beta-sheets and which are packed together by a hydrophobic core composed of residues from the zinc finger loop regions. The CCCC zinc finger is followed by a short alpha-helical stretch. The structural analysis revealed that the global fold of LIM1 closely resembles the recently determined solution structures of the carboxyl-terminal LIM2 domains of quail CRP2 and chicken CRP1, and that LIM1 and LIM2 are independently folded structural and presumably functional domains of CRP proteins. To explore the dynamical properties of CRP proteins, we have used 15N relaxation values (T1, T2, and nuclear Overhauser effect (NOE) to describe the dynamical behavior of a LIM domain. A model-free analysis revealed local variations in mobility along the backbone of the quail CRP2 LIM1 motif. Slow motions are evident in turn regions located between the various antiparallel beta-sheets or between their strands. By use of an extended motional model, fast backbone motions were detected for backbone amide NH groups of hydrophobic residues located in the core region of the LIM1 domain. These findings point to a flexible hydrophobic core in the LIM1 domain allowing residual relative mobility of the two zinc fingers, which might be important to optimize the LIM1 interface for interaction with its physiological target molecule(s) and to compensate enthalpically for the entropy loss upon binding.

-	~~{{STRUCTURE_1a7i\| PDB=1a7i \| SCENE= }}~~	+	Structure and intramodular dynamics of the amino-terminal LIM domain from quail cysteine- and glycine-rich protein CRP2.,Kontaxis G, Konrat R, Krautler B, Weiskirchen R, Bister K Biochemistry. 1998 May 19;37(20):7127-34. PMID:9585524<ref>PMID:9585524</ref>

-	~~===AMINO-TERMINAL LIM DOMAIN FROM QUAIL CYSTEINE AND GLYCINE-RICH PROTEIN~~, ~~NMR, MINIMIZED AVERAGE STRUCTURE===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_9585524}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1a7i]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Coturnix_japonica Coturnix japonica]~~. ~~Full experimental information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1A7I OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:009585524<~~/~~ref~~><~~ref group="xtra">PMID:009722554</ref><references group="xtra"~~/>	+
	[[Category: Coturnix japonica]]		[[Category: Coturnix japonica]]
	[[Category: Bister, K.]]		[[Category: Bister, K.]]