1jwd - Revision history

OCA at 08:39, 22 May 2024

OCA — Wed, 22 May 2024 08:39:29 GMT

←Older revision		Revision as of 08:39, 22 May 2024
Line 19:		Line 19:
	</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=1jwd 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=1jwd ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Calcyclin is a homodimeric protein belonging to the S100 subfamily of EF-hand Ca(2+)-binding proteins, which function in Ca(2+) signal transduction processes. A refined high-resolution solution structure of Ca(2+)-bound rabbit calcyclin has been determined by heteronuclear solution NMR. In order to understand the Ca(2+)-induced structural changes in S100 proteins, in-depth comparative structural analyses were used to compare the apo and Ca(2+)-bound states of calcyclin, the closely related S100B, and the prototypical Ca(2+)-sensor protein calmodulin. Upon Ca(2+) binding, the position and orientation of helix III in the second EF-hand is altered, whereas the rest of the protein, including the dimer interface, remains virtually unchanged. This Ca(2+)-induced structural change is much less drastic than the "opening" of the globular EF-hand domains that occurs in classical Ca(2+) sensors, such as calmodulin. Using homology models of calcyclin based on S100B, a binding site in calcyclin has been proposed for the N-terminal domain of annexin XI and the C-terminal domain of the neuronal calcyclin-binding protein. The structural basis for the specificity of S100 proteins is discussed in terms of the variation in sequence of critical contact residues in the common S100 target-binding site.
		+
		+	A structural basis for S100 protein specificity derived from comparative analysis of apo and Ca(2+)-calcyclin.,Maler L, Sastry M, Chazin WJ J Mol Biol. 2002 Mar 22;317(2):279-90. PMID:11902843<ref>PMID:11902843</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 1jwd" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[S100 proteins 3D structures\|S100 proteins 3D structures]]		*[[S100 proteins 3D structures\|S100 proteins 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 07:55, 3 April 2024

OCA — Wed, 03 Apr 2024 07:55:38 GMT

←Older revision		Revision as of 07:55, 3 April 2024
Line 1:		Line 1:

	==Ca2+-induced Structural Changes in Calcyclin: High-resolution Solution Structure of Ca2+-bound Calcyclin.==		==Ca2+-induced Structural Changes in Calcyclin: High-resolution Solution Structure of Ca2+-bound Calcyclin.==
-	<StructureSection load='1jwd' size='340' side='right'caption='[[1jwd~~]], [[NMR_Ensembles_of_Models \| 22 NMR models~~]]' scene=''>	+	<StructureSection load='1jwd' size='340' side='right'caption='[[1jwd]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1jwd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~European_rabbit European rabbit~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JWD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JWD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1jwd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JWD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JWD FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style='overflow: auto; max-height: 3em;'>[[1a03\|1a03]], [[2cnp\|2cnp]], [[1cnp\|1cnp]]</div></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">R-S100A6 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 European rabbit])~~</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=1jwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jwd OCA], [https://pdbe.org/1jwd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jwd RCSB], [https://www.ebi.ac.uk/pdbsum/1jwd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jwd 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=1jwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jwd OCA], [https://pdbe.org/1jwd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jwd RCSB], [https://www.ebi.ac.uk/pdbsum/1jwd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jwd ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/S10A6_RABIT S10A6_RABIT]] May function as calcium sensor and contribute to cellular calcium signaling (Potential). May function by interacting with other proteins and indirectly play a role in the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative (By similarity). Interacts with FKBP4 (By similarity).	+	[https://www.uniprot.org/uniprot/S10A6_RABIT S10A6_RABIT] May function as calcium sensor and contribute to cellular calcium signaling (Potential). May function by interacting with other proteins and indirectly play a role in the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative (By similarity). Interacts with FKBP4 (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 20:		Line 19:
	</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=1jwd 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=1jwd ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Calcyclin is a homodimeric protein belonging to the S100 subfamily of EF-hand Ca(2+)-binding proteins, which function in Ca(2+) signal transduction processes. A refined high-resolution solution structure of Ca(2+)-bound rabbit calcyclin has been determined by heteronuclear solution NMR. In order to understand the Ca(2+)-induced structural changes in S100 proteins, in-depth comparative structural analyses were used to compare the apo and Ca(2+)-bound states of calcyclin, the closely related S100B, and the prototypical Ca(2+)-sensor protein calmodulin. Upon Ca(2+) binding, the position and orientation of helix III in the second EF-hand is altered, whereas the rest of the protein, including the dimer interface, remains virtually unchanged. This Ca(2+)-induced structural change is much less drastic than the "opening" of the globular EF-hand domains that occurs in classical Ca(2+) sensors, such as calmodulin. Using homology models of calcyclin based on S100B, a binding site in calcyclin has been proposed for the N-terminal domain of annexin XI and the C-terminal domain of the neuronal calcyclin-binding protein. The structural basis for the specificity of S100 proteins is discussed in terms of the variation in sequence of critical contact residues in the common S100 target-binding site.
-
-	A structural basis for S100 protein specificity derived from comparative analysis of apo and Ca(2+)-calcyclin.,Maler L, Sastry M, Chazin WJ J Mol Biol. 2002 Mar 22;317(2):279-90. PMID:11902843<ref>PMID:11902843</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1jwd" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[S100 proteins 3D structures\|S100 proteins 3D structures]]		*[[S100 proteins 3D structures\|S100 proteins 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: European rabbit]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Chazin, W J~~]]	+	[[Category: Oryctolagus cuniculus]]
-	[[Category: ~~Maler, L~~]]	+	[[Category: Chazin WJ]]
-	[[Category: ~~Sastry, M~~]]	+	[[Category: Maler L]]
-	[[Category: ~~Ef-hand]]~~	+	[[Category: Sastry M]]
-	~~[[Category: Metal binding protein]]~~	+
-	~~[[Category: S100 protein]]~~	+
-	~~[[Category: S100a6~~]]	+

OCA at 08:05, 23 February 2022

OCA — Wed, 23 Feb 2022 08:05:57 GMT

←Older revision		Revision as of 08:05, 23 February 2022
Line 3:		Line 3:
	<StructureSection load='1jwd' size='340' side='right'caption='[[1jwd]], [[NMR_Ensembles_of_Models \| 22 NMR models]]' scene=''>		<StructureSection load='1jwd' size='340' side='right'caption='[[1jwd]], [[NMR_Ensembles_of_Models \| 22 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1jwd]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JWD OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1JWD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1jwd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JWD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JWD FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1a03\|1a03]], [[2cnp\|2cnp]], [[1cnp\|1cnp]]</div></td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1a03\|1a03]], [[2cnp\|2cnp]], [[1cnp\|1cnp]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">R-S100A6 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 European rabbit])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">R-S100A6 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 European rabbit])</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=1jwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jwd OCA], [~~http~~://pdbe.org/1jwd PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1jwd RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1jwd PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1jwd 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=1jwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jwd OCA], [https://pdbe.org/1jwd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jwd RCSB], [https://www.ebi.ac.uk/pdbsum/1jwd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jwd ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/S10A6_RABIT S10A6_RABIT]] May function as calcium sensor and contribute to cellular calcium signaling (Potential). May function by interacting with other proteins and indirectly play a role in the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative (By similarity). Interacts with FKBP4 (By similarity).	+	[[https://www.uniprot.org/uniprot/S10A6_RABIT S10A6_RABIT]] May function as calcium sensor and contribute to cellular calcium signaling (Potential). May function by interacting with other proteins and indirectly play a role in the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative (By similarity). Interacts with FKBP4 (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 07:36, 25 November 2020

OCA — Wed, 25 Nov 2020 07:36:53 GMT

←Older revision		Revision as of 07:36, 25 November 2020
Line 1:		Line 1:

	==Ca2+-induced Structural Changes in Calcyclin: High-resolution Solution Structure of Ca2+-bound Calcyclin.==		==Ca2+-induced Structural Changes in Calcyclin: High-resolution Solution Structure of Ca2+-bound Calcyclin.==
-	<StructureSection load='1jwd' size='340' side='right' caption='[[1jwd]], [[NMR_Ensembles_of_Models \| 22 NMR models]]' scene=''>	+	<StructureSection load='1jwd' size='340' side='right'caption='[[1jwd]], [[NMR_Ensembles_of_Models \| 22 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1jwd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JWD OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1JWD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1jwd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JWD OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1JWD FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a03\|1a03]], [[2cnp\|2cnp]], [[1cnp\|1cnp]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1a03\|1a03]], [[2cnp\|2cnp]], [[1cnp\|1cnp]]</div></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">R-S100A6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 European rabbit])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">R-S100A6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 European rabbit])</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=1jwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jwd OCA], [http://pdbe.org/1jwd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jwd RCSB], [http://www.ebi.ac.uk/pdbsum/1jwd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jwd ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1jwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jwd OCA], [http://pdbe.org/1jwd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jwd RCSB], [http://www.ebi.ac.uk/pdbsum/1jwd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jwd ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 29:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 1jwd" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1jwd" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[S100 proteins 3D structures\|S100 proteins 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 34:		Line 37:
	</StructureSection>		</StructureSection>
	[[Category: European rabbit]]		[[Category: European rabbit]]
		+	[[Category: Large Structures]]
	[[Category: Chazin, W J]]		[[Category: Chazin, W J]]
	[[Category: Maler, L]]		[[Category: Maler, L]]

OCA at 09:11, 17 January 2018

OCA — Wed, 17 Jan 2018 09:11:57 GMT

←Older revision		Revision as of 09:11, 17 January 2018
Line 1:		Line 1:
		+
	==Ca2+-induced Structural Changes in Calcyclin: High-resolution Solution Structure of Ca2+-bound Calcyclin.==		==Ca2+-induced Structural Changes in Calcyclin: High-resolution Solution Structure of Ca2+-bound Calcyclin.==
	<StructureSection load='1jwd' size='340' side='right' caption='[[1jwd]], [[NMR_Ensembles_of_Models \| 22 NMR models]]' scene=''>		<StructureSection load='1jwd' size='340' side='right' caption='[[1jwd]], [[NMR_Ensembles_of_Models \| 22 NMR models]]' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a03\|1a03]], [[2cnp\|2cnp]], [[1cnp\|1cnp]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a03\|1a03]], [[2cnp\|2cnp]], [[1cnp\|1cnp]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">R-S100A6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 European rabbit])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">R-S100A6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 European rabbit])</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=1jwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jwd OCA], [http://pdbe.org/1jwd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jwd RCSB], [http://www.ebi.ac.uk/pdbsum/1jwd 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=1jwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jwd OCA], [http://pdbe.org/1jwd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jwd RCSB], [http://www.ebi.ac.uk/pdbsum/1jwd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jwd ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 13:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jw/1jwd_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jw/1jwd_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 28:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 1jwd" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1jwd" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[S100 protein\|S100 protein]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:06, 9 February 2016

OCA — Tue, 09 Feb 2016 12:06:45 GMT

←Older revision		Revision as of 12:06, 9 February 2016
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=1jwd ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 22:05, 10 September 2015

OCA — Thu, 10 Sep 2015 22:05:19 GMT

←Older revision		Revision as of 22:05, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1jwd' size='340' side='right' caption='[[1jwd]], [[NMR_Ensembles_of_Models \| 22 NMR models]]' scene=''>		<StructureSection load='1jwd' size='340' side='right' caption='[[1jwd]], [[NMR_Ensembles_of_Models \| 22 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1jwd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Oryctolagus_cuniculus Oryctolagus cuniculus~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JWD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JWD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1jwd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JWD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JWD FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a03\|1a03]], [[2cnp\|2cnp]], [[1cnp\|1cnp]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a03\|1a03]], [[2cnp\|2cnp]], [[1cnp\|1cnp]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">R-S100A6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 ~~Oryctolagus cuniculus~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">R-S100A6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 European rabbit])</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=1jwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jwd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jwd RCSB], [http://www.ebi.ac.uk/pdbsum/1jwd 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=1jwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jwd OCA], [http://pdbe.org/1jwd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jwd RCSB], [http://www.ebi.ac.uk/pdbsum/1jwd PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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 1jwd" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 34:		Line 35:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Oryctolagus cuniculus~~]]	+	[[Category: European rabbit]]
	[[Category: Chazin, W J]]		[[Category: Chazin, W J]]
	[[Category: Maler, L]]		[[Category: Maler, L]]

OCA at 06:42, 25 December 2014

OCA — Thu, 25 Dec 2014 06:42:42 GMT

←Older revision		Revision as of 06:42, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1jwd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JWD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JWD FirstGlance]. <br>		<table><tr><td colspan='2'>[[1jwd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JWD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JWD FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a03\|1a03]], [[2cnp\|2cnp]], [[1cnp\|1cnp]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a03\|1a03]], [[2cnp\|2cnp]], [[1cnp\|1cnp]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">R-S100A6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 Oryctolagus cuniculus])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">R-S100A6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 Oryctolagus cuniculus])</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=1jwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jwd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jwd RCSB], [http://www.ebi.ac.uk/pdbsum/1jwd 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=1jwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jwd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jwd RCSB], [http://www.ebi.ac.uk/pdbsum/1jwd PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/S10A6_RABIT S10A6_RABIT]] May function as calcium sensor and contribute to cellular calcium signaling (Potential). May function by interacting with other proteins and indirectly play a role in the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative (By similarity). Interacts with FKBP4 (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 33:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: Oryctolagus cuniculus]]		[[Category: Oryctolagus cuniculus]]
-	[[Category: Chazin, W J.]]	+	[[Category: Chazin, W J]]
-	[[Category: Maler, L.]]	+	[[Category: Maler, L]]
-	[[Category: Sastry, M.]]	+	[[Category: Sastry, M]]
	[[Category: Ef-hand]]		[[Category: Ef-hand]]
	[[Category: Metal binding protein]]		[[Category: Metal binding protein]]
	[[Category: S100 protein]]		[[Category: S100 protein]]
	[[Category: S100a6]]		[[Category: S100a6]]

OCA at 14:30, 28 September 2014

OCA — Sun, 28 Sep 2014 14:30:20 GMT

←Older revision		Revision as of 14:30, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1jwd.~~png~~\|~~left~~\|200px]]	+	==Ca2+-induced Structural Changes in Calcyclin: High-resolution Solution Structure of Ca2+-bound Calcyclin.==
		+	<StructureSection load='1jwd' size='340' side='right' caption='[[1jwd]], [[NMR_Ensembles_of_Models \| 22 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1jwd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JWD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JWD FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a03\|1a03]], [[2cnp\|2cnp]], [[1cnp\|1cnp]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">R-S100A6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 Oryctolagus cuniculus])</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=1jwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jwd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jwd RCSB], [http://www.ebi.ac.uk/pdbsum/1jwd 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/jw/1jwd_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 ==
		+	Calcyclin is a homodimeric protein belonging to the S100 subfamily of EF-hand Ca(2+)-binding proteins, which function in Ca(2+) signal transduction processes. A refined high-resolution solution structure of Ca(2+)-bound rabbit calcyclin has been determined by heteronuclear solution NMR. In order to understand the Ca(2+)-induced structural changes in S100 proteins, in-depth comparative structural analyses were used to compare the apo and Ca(2+)-bound states of calcyclin, the closely related S100B, and the prototypical Ca(2+)-sensor protein calmodulin. Upon Ca(2+) binding, the position and orientation of helix III in the second EF-hand is altered, whereas the rest of the protein, including the dimer interface, remains virtually unchanged. This Ca(2+)-induced structural change is much less drastic than the "opening" of the globular EF-hand domains that occurs in classical Ca(2+) sensors, such as calmodulin. Using homology models of calcyclin based on S100B, a binding site in calcyclin has been proposed for the N-terminal domain of annexin XI and the C-terminal domain of the neuronal calcyclin-binding protein. The structural basis for the specificity of S100 proteins is discussed in terms of the variation in sequence of critical contact residues in the common S100 target-binding site.

-	~~{{STRUCTURE_1jwd\| PDB=1jwd \| SCENE= }}~~	+	A structural basis for S100 protein specificity derived from comparative analysis of apo and Ca(2+)-calcyclin.,Maler L, Sastry M, Chazin WJ J Mol Biol. 2002 Mar 22;317(2):279-90. PMID:11902843<ref>PMID:11902843</ref>

-	~~===Ca2+-induced Structural Changes in Calcyclin: High-resolution Solution Structure~~ of ~~Ca2+-bound Calcyclin~~.~~===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_11902843}}~~	+	==See Also==
-		+	*[[S100 protein\|S100 protein]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~1jwd~~]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JWD OCA].	+	<references/>
-		+	__TOC__
-	==~~Reference~~==	+	</StructureSection>
-	<~~ref group="xtra">PMID:011902843<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Oryctolagus cuniculus]]		[[Category: Oryctolagus cuniculus]]
	[[Category: Chazin, W J.]]		[[Category: Chazin, W J.]]

OCA: Protected "1jwd" [edit=sysop:move=sysop]

OCA — Wed, 05 Dec 2012 11:25:43 GMT

Protected "1jwd" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:25, 5 December 2012