1sym - Revision history

OCA at 09:10, 22 May 2024

OCA — Wed, 22 May 2024 09:10:56 GMT

←Older revision		Revision as of 09:10, 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=1sym 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=1sym ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	S100B(beta beta), a member of the S100 protein family, is a Ca(2+)-binding protein with noncovalent interactions at its dimer interface. Each apo-S100 beta subunit (91 residues) has four alpha-helices and a small antiparallel beta-sheet, consistent with two predicted helix-loop-helix Ca(2+)-binding domains known as EF-hands [Amburgey et al. (1995) J. Biomol. NMR 6, 171-179]. The three-dimensional solution structure of apo-S100B(beta beta) from rat has been determined using 2672 distance (14.7 per residue) and 88 dihedral angle restraints derived from multidimensional nuclear magnetic resonance spectroscopy. Apo-S100B (beta beta) is found to be globular and compact with an extensive hydrophobic core and a highly charged surface, consistent with its high solubility. At the symmetric dimer interface, 172 intermolecular nuclear Overhauser effect correlations (NOEs) define the antiparallel alignment of helix I with I' and of helix IV with IV'. The perpendicular association of these pairs of antiparallel helices forms an X-type four-helical bundle at the dimer interface. Whereas, the four helices within each apo-S100 beta subunit adopt a unicornate-type four-helix bundle, with helix I protruding from the parallel bundle of helices II, III, and IV. Accordingly, the orientation of helix III relative to helices I, II, and IV in each subunit differs significantly from that known for other Ca(2+)-binding proteins. Indeed, the interhelical angle (omega) observed in the C-terminal EF-hand of apo-S100 beta is -142 degrees, whereas omega ranges from 118 degrees to 145 degrees in the apo state and from 84 degrees to 128 degrees in the Ca(2+)-bound state for the EF-hands of calbindin D9k, calcyclin, and calmodulin. Thus, a significant conformational change in the C-terminal EF-hand would be required for it to adopt a structure typical of the Ca(2+)-bound state, which could readily explain the dramatic spectral effects observed upon the addition of Ca2+ to apo-S100B(beta beta).
		+
		+	Solution structure of rat apo-S100B(beta beta) as determined by NMR spectroscopy.,Drohat AC, Amburgey JC, Abildgaard F, Starich MR, Baldisseri D, Weber DJ Biochemistry. 1996 Sep 10;35(36):11577-88. PMID:8794737<ref>PMID:8794737</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 1sym" style="background-color:#fffaf0;"></div>

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

OCA at 08:36, 1 May 2024

OCA — Wed, 01 May 2024 08:36:31 GMT

←Older revision		Revision as of 08:36, 1 May 2024
Line 1:		Line 1:

	==3-D SOLUTION STRUCTURE OF REDUCED APO-S100B FROM RAT, NMR, 20 STRUCTURES==		==3-D SOLUTION STRUCTURE OF REDUCED APO-S100B FROM RAT, NMR, 20 STRUCTURES==
-	<StructureSection load='1sym' size='340' side='right'caption='[[1sym~~]], [[NMR_Ensembles_of_Models \| 20 NMR models~~]]' scene=''>	+	<StructureSection load='1sym' size='340' side='right'caption='[[1sym]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1sym]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Buffalo_rat Buffalo rat~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SYM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SYM FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1sym]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SYM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SYM FirstGlance]. <br>
-	</td></tr><tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>S100BETA FROM RATTUS NORVEGICU ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~10116 Buffalo rat])~~</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sym OCA], [https://pdbe.org/1sym PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sym RCSB], [https://www.ebi.ac.uk/pdbsum/1sym PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sym 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=1sym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sym OCA], [https://pdbe.org/1sym PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sym RCSB], [https://www.ebi.ac.uk/pdbsum/1sym PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sym ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/S100B_RAT S100B_RAT]] Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling. Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization.<ref>PMID:19910580</ref> <ref>PMID:20351179</ref>	+	[https://www.uniprot.org/uniprot/S100B_RAT S100B_RAT] Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling. Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization.<ref>PMID:19910580</ref> <ref>PMID:20351179</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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=1sym 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=1sym ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	S100B(beta beta), a member of the S100 protein family, is a Ca(2+)-binding protein with noncovalent interactions at its dimer interface. Each apo-S100 beta subunit (91 residues) has four alpha-helices and a small antiparallel beta-sheet, consistent with two predicted helix-loop-helix Ca(2+)-binding domains known as EF-hands [Amburgey et al. (1995) J. Biomol. NMR 6, 171-179]. The three-dimensional solution structure of apo-S100B(beta beta) from rat has been determined using 2672 distance (14.7 per residue) and 88 dihedral angle restraints derived from multidimensional nuclear magnetic resonance spectroscopy. Apo-S100B (beta beta) is found to be globular and compact with an extensive hydrophobic core and a highly charged surface, consistent with its high solubility. At the symmetric dimer interface, 172 intermolecular nuclear Overhauser effect correlations (NOEs) define the antiparallel alignment of helix I with I' and of helix IV with IV'. The perpendicular association of these pairs of antiparallel helices forms an X-type four-helical bundle at the dimer interface. Whereas, the four helices within each apo-S100 beta subunit adopt a unicornate-type four-helix bundle, with helix I protruding from the parallel bundle of helices II, III, and IV. Accordingly, the orientation of helix III relative to helices I, II, and IV in each subunit differs significantly from that known for other Ca(2+)-binding proteins. Indeed, the interhelical angle (omega) observed in the C-terminal EF-hand of apo-S100 beta is -142 degrees, whereas omega ranges from 118 degrees to 145 degrees in the apo state and from 84 degrees to 128 degrees in the Ca(2+)-bound state for the EF-hands of calbindin D9k, calcyclin, and calmodulin. Thus, a significant conformational change in the C-terminal EF-hand would be required for it to adopt a structure typical of the Ca(2+)-bound state, which could readily explain the dramatic spectral effects observed upon the addition of Ca2+ to apo-S100B(beta beta).
-
-	Solution structure of rat apo-S100B(beta beta) as determined by NMR spectroscopy.,Drohat AC, Amburgey JC, Abildgaard F, Starich MR, Baldisseri D, Weber DJ Biochemistry. 1996 Sep 10;35(36):11577-88. PMID:8794737<ref>PMID:8794737</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1sym" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Buffalo rat]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Drohat, A C~~]]	+	[[Category: Rattus norvegicus]]
-	[[Category: ~~Weber, D J~~]]	+	[[Category: Drohat AC]]
-	[[Category: ~~Calcium-binding protein]]~~	+	[[Category: Weber DJ]]
-	~~[[Category: Metal-binding~~]]	+

OCA at 06:37, 2 March 2022

OCA — Wed, 02 Mar 2022 06:37:54 GMT

←Older revision		Revision as of 06:37, 2 March 2022
Line 3:		Line 3:
	<StructureSection load='1sym' size='340' side='right'caption='[[1sym]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='1sym' size='340' side='right'caption='[[1sym]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1sym]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SYM OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1SYM FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1sym]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SYM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SYM FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">S100BETA FROM RATTUS NORVEGICU ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">S100BETA FROM RATTUS NORVEGICU ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=1sym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sym OCA], [~~http~~://pdbe.org/1sym PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1sym RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1sym PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1sym 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=1sym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sym OCA], [https://pdbe.org/1sym PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sym RCSB], [https://www.ebi.ac.uk/pdbsum/1sym PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sym ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/S100B_RAT S100B_RAT]] Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling. Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization.<ref>PMID:19910580</ref> <ref>PMID:20351179</ref>	+	[[https://www.uniprot.org/uniprot/S100B_RAT S100B_RAT]] Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling. Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization.<ref>PMID:19910580</ref> <ref>PMID:20351179</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 11:36, 24 December 2020

OCA — Thu, 24 Dec 2020 11:36:36 GMT

←Older revision		Revision as of 11:36, 24 December 2020
Line 1:		Line 1:

	==3-D SOLUTION STRUCTURE OF REDUCED APO-S100B FROM RAT, NMR, 20 STRUCTURES==		==3-D SOLUTION STRUCTURE OF REDUCED APO-S100B FROM RAT, NMR, 20 STRUCTURES==
-	<StructureSection load='1sym' size='340' side='right' caption='[[1sym]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>	+	<StructureSection load='1sym' size='340' side='right'caption='[[1sym]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1sym]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SYM OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1SYM FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1sym]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SYM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1SYM FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">S100BETA FROM RATTUS NORVEGICU ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">S100BETA FROM RATTUS NORVEGICU ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=1sym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sym OCA], [http://pdbe.org/1sym PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sym RCSB], [http://www.ebi.ac.uk/pdbsum/1sym PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1sym 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=1sym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sym OCA], [http://pdbe.org/1sym PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sym RCSB], [http://www.ebi.ac.uk/pdbsum/1sym PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1sym ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 30:		Line 30:

	==See Also==		==See Also==
-	*[[S100 ~~protein~~\|S100 ~~protein~~]]	+	*[[S100 proteins 3D structures\|S100 proteins 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 36:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Buffalo rat]]		[[Category: Buffalo rat]]
		+	[[Category: Large Structures]]
	[[Category: Drohat, A C]]		[[Category: Drohat, A C]]
	[[Category: Weber, D J]]		[[Category: Weber, D J]]
	[[Category: Calcium-binding protein]]		[[Category: Calcium-binding protein]]
	[[Category: Metal-binding]]		[[Category: Metal-binding]]

OCA at 07:25, 14 March 2018

OCA — Wed, 14 Mar 2018 07:25:54 GMT

←Older revision		Revision as of 07:25, 14 March 2018
Line 1:		Line 1:
		+
	==3-D SOLUTION STRUCTURE OF REDUCED APO-S100B FROM RAT, NMR, 20 STRUCTURES==		==3-D SOLUTION STRUCTURE OF REDUCED APO-S100B FROM RAT, NMR, 20 STRUCTURES==
	<StructureSection load='1sym' size='340' side='right' caption='[[1sym]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='1sym' size='340' side='right' caption='[[1sym]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[1sym]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SYM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SYM FirstGlance]. <br>		<table><tr><td colspan='2'>[[1sym]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SYM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SYM FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">S100BETA FROM RATTUS NORVEGICU ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">S100BETA FROM RATTUS NORVEGICU ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=1sym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sym OCA], [http://pdbe.org/1sym PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sym RCSB], [http://www.ebi.ac.uk/pdbsum/1sym 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=1sym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sym OCA], [http://pdbe.org/1sym PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sym RCSB], [http://www.ebi.ac.uk/pdbsum/1sym PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1sym ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 12:		Line 13:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sy/1sym_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sy/1sym_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>
	</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=1sym ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 08:59, 11 September 2015

OCA — Fri, 11 Sep 2015 08:59:06 GMT

←Older revision		Revision as of 08:59, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1sym' size='340' side='right' caption='[[1sym]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='1sym' size='340' side='right' caption='[[1sym]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1sym]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Rattus_norvegicus Rattus norvegicus~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SYM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SYM FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1sym]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SYM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SYM FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">S100BETA FROM RATTUS NORVEGICU ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 ~~Rattus norvegicus~~])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">S100BETA FROM RATTUS NORVEGICU ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=1sym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sym OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1sym RCSB], [http://www.ebi.ac.uk/pdbsum/1sym 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=1sym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sym OCA], [http://pdbe.org/1sym PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sym RCSB], [http://www.ebi.ac.uk/pdbsum/1sym PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 26:		Line 26:
	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 1sym" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 33:		Line 34:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Rattus norvegicus~~]]	+	[[Category: Buffalo rat]]
	[[Category: Drohat, A C]]		[[Category: Drohat, A C]]
	[[Category: Weber, D J]]		[[Category: Weber, D J]]
	[[Category: Calcium-binding protein]]		[[Category: Calcium-binding protein]]
	[[Category: Metal-binding]]		[[Category: Metal-binding]]

OCA at 14:10, 25 December 2014

OCA — Thu, 25 Dec 2014 14:10:52 GMT

←Older revision		Revision as of 14:10, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1sym]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SYM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SYM FirstGlance]. <br>		<table><tr><td colspan='2'>[[1sym]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SYM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SYM FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">S100BETA FROM RATTUS NORVEGICU ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">S100BETA FROM RATTUS NORVEGICU ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</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=1sym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sym OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1sym RCSB], [http://www.ebi.ac.uk/pdbsum/1sym 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=1sym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sym OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1sym RCSB], [http://www.ebi.ac.uk/pdbsum/1sym PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/S100B_RAT S100B_RAT]] Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling. Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization.<ref>PMID:19910580</ref> <ref>PMID:20351179</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 34:
	</StructureSection>		</StructureSection>
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
-	[[Category: Drohat, A C.]]	+	[[Category: Drohat, A C]]
-	[[Category: Weber, D J.]]	+	[[Category: Weber, D J]]
	[[Category: Calcium-binding protein]]		[[Category: Calcium-binding protein]]
	[[Category: Metal-binding]]		[[Category: Metal-binding]]

OCA at 16:47, 29 September 2014

OCA — Mon, 29 Sep 2014 16:47:21 GMT

←Older revision		Revision as of 16:47, 29 September 2014
Line 1:		Line 1:
-	[[~~Image~~:1sym.~~png\|left~~\|200px]]	+	==3-D SOLUTION STRUCTURE OF REDUCED APO-S100B FROM RAT, NMR, 20 STRUCTURES==
		+	<StructureSection load='1sym' size='340' side='right' caption='[[1sym]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1sym]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SYM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SYM FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">S100BETA FROM RATTUS NORVEGICU ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</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=1sym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sym OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1sym RCSB], [http://www.ebi.ac.uk/pdbsum/1sym 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/sy/1sym_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 ==
		+	S100B(beta beta), a member of the S100 protein family, is a Ca(2+)-binding protein with noncovalent interactions at its dimer interface. Each apo-S100 beta subunit (91 residues) has four alpha-helices and a small antiparallel beta-sheet, consistent with two predicted helix-loop-helix Ca(2+)-binding domains known as EF-hands [Amburgey et al. (1995) J. Biomol. NMR 6, 171-179]. The three-dimensional solution structure of apo-S100B(beta beta) from rat has been determined using 2672 distance (14.7 per residue) and 88 dihedral angle restraints derived from multidimensional nuclear magnetic resonance spectroscopy. Apo-S100B (beta beta) is found to be globular and compact with an extensive hydrophobic core and a highly charged surface, consistent with its high solubility. At the symmetric dimer interface, 172 intermolecular nuclear Overhauser effect correlations (NOEs) define the antiparallel alignment of helix I with I' and of helix IV with IV'. The perpendicular association of these pairs of antiparallel helices forms an X-type four-helical bundle at the dimer interface. Whereas, the four helices within each apo-S100 beta subunit adopt a unicornate-type four-helix bundle, with helix I protruding from the parallel bundle of helices II, III, and IV. Accordingly, the orientation of helix III relative to helices I, II, and IV in each subunit differs significantly from that known for other Ca(2+)-binding proteins. Indeed, the interhelical angle (omega) observed in the C-terminal EF-hand of apo-S100 beta is -142 degrees, whereas omega ranges from 118 degrees to 145 degrees in the apo state and from 84 degrees to 128 degrees in the Ca(2+)-bound state for the EF-hands of calbindin D9k, calcyclin, and calmodulin. Thus, a significant conformational change in the C-terminal EF-hand would be required for it to adopt a structure typical of the Ca(2+)-bound state, which could readily explain the dramatic spectral effects observed upon the addition of Ca2+ to apo-S100B(beta beta).

-	~~{{STRUCTURE_1sym\| PDB=1sym \| SCENE= }}~~	+	Solution structure of rat apo-S100B(beta beta) as determined by NMR spectroscopy.,Drohat AC, Amburgey JC, Abildgaard F, Starich MR, Baldisseri D, Weber DJ Biochemistry. 1996 Sep 10;35(36):11577-88. PMID:8794737<ref>PMID:8794737</ref>

-	~~===3-D SOLUTION STRUCTURE OF REDUCED APO-S100B FROM RAT~~, ~~NMR, 20 STRUCTURES===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_8794737}}~~	+	==See Also==
-		+	*[[S100 protein\|S100 protein]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~1sym~~]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SYM OCA].	+	<references/>
-		+	__TOC__
-	==~~Reference~~==	+	</StructureSection>
-	<~~ref group="xtra">PMID:008794737<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
	[[Category: Drohat, A C.]]		[[Category: Drohat, A C.]]

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

OCA — Sat, 05 Jan 2013 12:22:41 GMT

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

←Older revision

Revision as of 12:22, 5 January 2013

OCA at 12:22, 5 January 2013

OCA — Sat, 05 Jan 2013 12:22:39 GMT

←Older revision		Revision as of 12:22, 5 January 2013
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1sym.png\|left\|200px]]		[[Image:1sym.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1sym", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_1sym\| PDB=1sym \| SCENE= }}		{{STRUCTURE_1sym\| PDB=1sym \| SCENE= }}

	===3-D SOLUTION STRUCTURE OF REDUCED APO-S100B FROM RAT, NMR, 20 STRUCTURES===		===3-D SOLUTION STRUCTURE OF REDUCED APO-S100B FROM RAT, NMR, 20 STRUCTURES===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_8794737}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 8794737 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_8794737}}		{{ABSTRACT_PUBMED_8794737}}

	==About this Structure==		==About this Structure==
-	~~1SYM~~ is a 2 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SYM OCA].	+	[[1sym]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SYM OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~8794737~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:008794737</ref><references group="xtra"/>
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
	[[Category: Drohat, A C.]]		[[Category: Drohat, A C.]]
Line 29:		Line 17:
	[[Category: Calcium-binding protein]]		[[Category: Calcium-binding protein]]
	[[Category: Metal-binding]]		[[Category: Metal-binding]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 18:20:25 2009''