1mwn - Revision history

OCA at 08:51, 22 May 2024

OCA — Wed, 22 May 2024 08:51:33 GMT

←Older revision		Revision as of 08:51, 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=1mwn 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=1mwn ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The solution NMR structure is reported for Ca(2+)-loaded S100B bound to a 12-residue peptide, TRTK-12, from the actin capping protein CapZ (alpha1 or alpha2 subunit, residues 265-276: TRTKIDWNKILS). This peptide was discovered by Dimlich and co-workers by screening a bacteriophage random peptide display library, and it matches exactly the consensus S100B binding sequence ((K/R)(L/I)XWXXIL). As with other S100B target proteins, a calcium-dependent conformational change in S100B is required for TRTK-12 binding. The TRTK-12 peptide is an amphipathic helix (residues W7 to S12) in the S100B-TRTK complex, and helix 4 of S100B is extended by three or four residues upon peptide binding. However, helical TRTK-12 in the S100B-peptide complex is uniquely oriented when compared to the three-dimensional structures of other S100-peptide complexes. The three-dimensional structure of the S100B-TRTK peptide complex illustrates that residues in the S100B binding consensus sequence (K4, I5, W7, I10, L11) are all involved in the S100B-peptide interface, which can explain its orientation in the S100B binding pocket and its relatively high binding affinity. A comparison of the S100B-TRTK peptide structure to the structures of apo- and Ca(2+)-bound S100B illustrates that the binding site of TRTK-12 is buried in apo-S100B, but is exposed in Ca(2+)-bound S100B as necessary to bind the TRTK-12 peptide.
		+
		+	Solution NMR structure of S100B bound to the high-affinity target peptide TRTK-12.,Inman KG, Yang R, Rustandi RR, Miller KE, Baldisseri DM, Weber DJ J Mol Biol. 2002 Dec 13;324(5):1003-14. PMID:12470955<ref>PMID:12470955</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 1mwn" style="background-color:#fffaf0;"></div>

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

OCA at 08:42, 10 April 2024

OCA — Wed, 10 Apr 2024 08:42:51 GMT

←Older revision		Revision as of 08:42, 10 April 2024
Line 1:		Line 1:

	==Solution NMR structure of S100B bound to the high-affinity target peptide TRTK-12==		==Solution NMR structure of S100B bound to the high-affinity target peptide TRTK-12==
-	<StructureSection load='1mwn' size='340' side='right'caption='[[1mwn~~]], [[NMR_Ensembles_of_Models \| 20 NMR models~~]]' scene=''>	+	<StructureSection load='1mwn' size='340' side='right'caption='[[1mwn]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1mwn]] is a 4 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=1MWN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MWN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1mwn]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MWN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MWN FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CA:CALCIUM+ION'>CA</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='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style~~=~~'overflow: auto; max-height: 3em;'~~>~~[[1dt7\|1dt7]]~~<~~/div></td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b~~></td>~~<td class="sblockDat">S100B ([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'>[https://proteopedia.org/fgij/fg.htm?mol=1mwn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mwn OCA], [https://pdbe.org/1mwn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mwn RCSB], [https://www.ebi.ac.uk/pdbsum/1mwn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mwn 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=1mwn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mwn OCA], [https://pdbe.org/1mwn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mwn RCSB], [https://www.ebi.ac.uk/pdbsum/1mwn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mwn 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/CAZA1_HUMAN CAZA1_HUMAN]] F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.	+	[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 21:		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=1mwn 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=1mwn ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The solution NMR structure is reported for Ca(2+)-loaded S100B bound to a 12-residue peptide, TRTK-12, from the actin capping protein CapZ (alpha1 or alpha2 subunit, residues 265-276: TRTKIDWNKILS). This peptide was discovered by Dimlich and co-workers by screening a bacteriophage random peptide display library, and it matches exactly the consensus S100B binding sequence ((K/R)(L/I)XWXXIL). As with other S100B target proteins, a calcium-dependent conformational change in S100B is required for TRTK-12 binding. The TRTK-12 peptide is an amphipathic helix (residues W7 to S12) in the S100B-TRTK complex, and helix 4 of S100B is extended by three or four residues upon peptide binding. However, helical TRTK-12 in the S100B-peptide complex is uniquely oriented when compared to the three-dimensional structures of other S100-peptide complexes. The three-dimensional structure of the S100B-TRTK peptide complex illustrates that residues in the S100B binding consensus sequence (K4, I5, W7, I10, L11) are all involved in the S100B-peptide interface, which can explain its orientation in the S100B binding pocket and its relatively high binding affinity. A comparison of the S100B-TRTK peptide structure to the structures of apo- and Ca(2+)-bound S100B illustrates that the binding site of TRTK-12 is buried in apo-S100B, but is exposed in Ca(2+)-bound S100B as necessary to bind the TRTK-12 peptide.
-
-	Solution NMR structure of S100B bound to the high-affinity target peptide TRTK-12.,Inman KG, Yang R, Rustandi RR, Miller KE, Baldisseri DM, Weber DJ J Mol Biol. 2002 Dec 13;324(5):1003-14. PMID:12470955<ref>PMID:12470955</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1mwn" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 37:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Buffalo rat~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Baldisseri~~, D M~~]]	+	[[Category: Rattus norvegicus]]
-	[[Category: Inman~~, K G~~]]	+	[[Category: Baldisseri DM]]
-	[[Category: Miller~~, K E~~]]	+	[[Category: Inman KG]]
-	[[Category: Rustandi~~, R R~~]]	+	[[Category: Miller KE]]
-	[[Category: Weber~~, D J~~]]	+	[[Category: Rustandi RR]]
-	[[Category: Yang, R]]	+	[[Category: Weber DJ]]
-	~~[[Category: 20 structure]]~~	+	[[Category: Yang R]]
-	~~[[Category: Calcium-binding]]~~	+
-	~~[[Category: Ef-hand]]~~	+
-	~~[[Category: Four helix bundle]]~~	+
-	~~[[Category: Helix loop helix]]~~	+
-	~~[[Category: Protein-peptide complex]]~~	+
-	~~[[Category: S100 protein]]~~	+
-	~~[[Category: S100b]]~~	+
-	~~[[Category: Structural protein]]~~	+
-	~~[[Category: Trtk-12~~]]	+

OCA at 08:19, 23 February 2022

OCA — Wed, 23 Feb 2022 08:19:30 GMT

←Older revision		Revision as of 08:19, 23 February 2022
Line 3:		Line 3:
	<StructureSection load='1mwn' size='340' side='right'caption='[[1mwn]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='1mwn' size='340' side='right'caption='[[1mwn]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1mwn]] is a 4 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=1MWN OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1MWN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1mwn]] is a 4 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=1MWN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MWN FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dt7\|1dt7]]</div></td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dt7\|1dt7]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">S100B ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">S100B ([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=1mwn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mwn OCA], [~~http~~://pdbe.org/1mwn PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1mwn RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1mwn PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1mwn 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=1mwn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mwn OCA], [https://pdbe.org/1mwn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mwn RCSB], [https://www.ebi.ac.uk/pdbsum/1mwn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mwn 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> [[~~http~~://www.uniprot.org/uniprot/CAZA1_HUMAN CAZA1_HUMAN]] F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.	+	[[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/CAZA1_HUMAN CAZA1_HUMAN]] F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 08:42, 2 December 2020

OCA — Wed, 02 Dec 2020 08:42:05 GMT

←Older revision		Revision as of 08:42, 2 December 2020
Line 1:		Line 1:

	==Solution NMR structure of S100B bound to the high-affinity target peptide TRTK-12==		==Solution NMR structure of S100B bound to the high-affinity target peptide TRTK-12==
-	<StructureSection load='1mwn' size='340' side='right' caption='[[1mwn]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>	+	<StructureSection load='1mwn' size='340' side='right'caption='[[1mwn]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1mwn]] is a 4 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=1MWN OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1MWN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1mwn]] is a 4 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=1MWN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1MWN FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dt7\|1dt7]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dt7\|1dt7]]</div></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">S100B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">S100B ([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=1mwn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mwn OCA], [http://pdbe.org/1mwn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mwn RCSB], [http://www.ebi.ac.uk/pdbsum/1mwn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mwn 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=1mwn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mwn OCA], [http://pdbe.org/1mwn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mwn RCSB], [http://www.ebi.ac.uk/pdbsum/1mwn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mwn ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 15:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mw/1mwn_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mw/1mwn_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 30:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1mwn" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1mwn" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[S100 proteins 3D structures\|S100 proteins 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 35:		Line 38:
	</StructureSection>		</StructureSection>
	[[Category: Buffalo rat]]		[[Category: Buffalo rat]]
		+	[[Category: Large Structures]]
	[[Category: Baldisseri, D M]]		[[Category: Baldisseri, D M]]
	[[Category: Inman, K G]]		[[Category: Inman, K G]]

OCA at 10:13, 25 October 2017

OCA — Wed, 25 Oct 2017 10:13:04 GMT

←Older revision		Revision as of 10:13, 25 October 2017
Line 1:		Line 1:
		+
	==Solution NMR structure of S100B bound to the high-affinity target peptide TRTK-12==		==Solution NMR structure of S100B bound to the high-affinity target peptide TRTK-12==
	<StructureSection load='1mwn' size='340' side='right' caption='[[1mwn]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='1mwn' size='340' side='right' caption='[[1mwn]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dt7\|1dt7]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dt7\|1dt7]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">S100B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">S100B ([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=1mwn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mwn OCA], [http://pdbe.org/1mwn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mwn RCSB], [http://www.ebi.ac.uk/pdbsum/1mwn 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=1mwn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mwn OCA], [http://pdbe.org/1mwn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mwn RCSB], [http://www.ebi.ac.uk/pdbsum/1mwn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mwn ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	<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=1mwn ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 29:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1mwn" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1mwn" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[S100 protein\|S100 protein]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 15:52, 11 September 2015

OCA — Fri, 11 Sep 2015 15:52:26 GMT

←Older revision		Revision as of 15:52, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1mwn' size='340' side='right' caption='[[1mwn]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='1mwn' size='340' side='right' caption='[[1mwn]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1mwn]] is a 4 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=1MWN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MWN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1mwn]] is a 4 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=1MWN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MWN FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dt7\|1dt7]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dt7\|1dt7]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">S100B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 ~~Rattus norvegicus~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">S100B ([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=1mwn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mwn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mwn RCSB], [http://www.ebi.ac.uk/pdbsum/1mwn 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=1mwn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mwn OCA], [http://pdbe.org/1mwn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mwn RCSB], [http://www.ebi.ac.uk/pdbsum/1mwn PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 28:		Line 28:
	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 1mwn" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Rattus norvegicus~~]]	+	[[Category: Buffalo rat]]
	[[Category: Baldisseri, D M]]		[[Category: Baldisseri, D M]]
	[[Category: Inman, K G]]		[[Category: Inman, K G]]

OCA at 18:38, 25 December 2014

OCA — Thu, 25 Dec 2014 18:38:14 GMT

←Older revision		Revision as of 18:38, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1mwn]] is a 4 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=1MWN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MWN FirstGlance]. <br>		<table><tr><td colspan='2'>[[1mwn]] is a 4 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=1MWN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MWN FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dt7\|1dt7]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dt7\|1dt7]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">S100B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">S100B ([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=1mwn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mwn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mwn RCSB], [http://www.ebi.ac.uk/pdbsum/1mwn 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=1mwn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mwn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mwn RCSB], [http://www.ebi.ac.uk/pdbsum/1mwn 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> [[http://www.uniprot.org/uniprot/CAZA1_HUMAN CAZA1_HUMAN]] F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 34:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
-	[[Category: Baldisseri, D M.]]	+	[[Category: Baldisseri, D M]]
-	[[Category: Inman, K G.]]	+	[[Category: Inman, K G]]
-	[[Category: Miller, K E.]]	+	[[Category: Miller, K E]]
-	[[Category: Rustandi, R R.]]	+	[[Category: Rustandi, R R]]
-	[[Category: Weber, D J.]]	+	[[Category: Weber, D J]]
-	[[Category: Yang, R.]]	+	[[Category: Yang, R]]
	[[Category: 20 structure]]		[[Category: 20 structure]]
	[[Category: Calcium-binding]]		[[Category: Calcium-binding]]

OCA at 17:46, 28 September 2014

OCA — Sun, 28 Sep 2014 17:46:34 GMT

←Older revision		Revision as of 17:46, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1mwn.~~png~~\|~~left~~\|200px]]	+	==Solution NMR structure of S100B bound to the high-affinity target peptide TRTK-12==
		+	<StructureSection load='1mwn' size='340' side='right' caption='[[1mwn]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1mwn]] is a 4 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=1MWN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MWN FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dt7\|1dt7]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">S100B ([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=1mwn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mwn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mwn RCSB], [http://www.ebi.ac.uk/pdbsum/1mwn 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/mw/1mwn_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 ==
		+	The solution NMR structure is reported for Ca(2+)-loaded S100B bound to a 12-residue peptide, TRTK-12, from the actin capping protein CapZ (alpha1 or alpha2 subunit, residues 265-276: TRTKIDWNKILS). This peptide was discovered by Dimlich and co-workers by screening a bacteriophage random peptide display library, and it matches exactly the consensus S100B binding sequence ((K/R)(L/I)XWXXIL). As with other S100B target proteins, a calcium-dependent conformational change in S100B is required for TRTK-12 binding. The TRTK-12 peptide is an amphipathic helix (residues W7 to S12) in the S100B-TRTK complex, and helix 4 of S100B is extended by three or four residues upon peptide binding. However, helical TRTK-12 in the S100B-peptide complex is uniquely oriented when compared to the three-dimensional structures of other S100-peptide complexes. The three-dimensional structure of the S100B-TRTK peptide complex illustrates that residues in the S100B binding consensus sequence (K4, I5, W7, I10, L11) are all involved in the S100B-peptide interface, which can explain its orientation in the S100B binding pocket and its relatively high binding affinity. A comparison of the S100B-TRTK peptide structure to the structures of apo- and Ca(2+)-bound S100B illustrates that the binding site of TRTK-12 is buried in apo-S100B, but is exposed in Ca(2+)-bound S100B as necessary to bind the TRTK-12 peptide.

-	~~{{STRUCTURE_1mwn\| PDB=1mwn \| SCENE= }}~~	+	Solution NMR structure of S100B bound to the high-affinity target peptide TRTK-12.,Inman KG, Yang R, Rustandi RR, Miller KE, Baldisseri DM, Weber DJ J Mol Biol. 2002 Dec 13;324(5):1003-14. PMID:12470955<ref>PMID:12470955</ref>

-	~~===Solution NMR structure~~ of ~~S100B bound to~~ the ~~high-affinity target peptide TRTK-12===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_12470955}}~~	+	==See Also==
-		+	*[[S100 protein\|S100 protein]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~1mwn~~]] is a 4 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=1MWN OCA].	+	<references/>
-		+	__TOC__
-	==~~Reference~~==	+	</StructureSection>
-	<~~ref group="xtra">PMID:012470955<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
	[[Category: Baldisseri, D M.]]		[[Category: Baldisseri, D M.]]

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

OCA — Wed, 05 Dec 2012 20:43:02 GMT

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

←Older revision

Revision as of 20:43, 5 December 2012

OCA at 20:43, 5 December 2012

OCA — Wed, 05 Dec 2012 20:43:00 GMT

←Older revision		Revision as of 20:43, 5 December 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1mwn.png\|left\|200px]]		[[Image:1mwn.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1mwn", 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_1mwn\| PDB=1mwn \| SCENE= }}		{{STRUCTURE_1mwn\| PDB=1mwn \| SCENE= }}

	===Solution NMR structure of S100B bound to the high-affinity target peptide TRTK-12===		===Solution NMR structure of S100B bound to the high-affinity target peptide TRTK-12===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_12470955}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 12470955 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_12470955}}		{{ABSTRACT_PUBMED_12470955}}

	==About this Structure==		==About this Structure==
-	~~1MWN~~ is a 4 ~~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=1MWN OCA].	+	[[1mwn]] is a 4 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=1MWN OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~12470955~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:012470955</ref><references group="xtra"/>
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
	[[Category: Baldisseri, D M.]]		[[Category: Baldisseri, D M.]]
Line 36:		Line 24:
	[[Category: Four helix bundle]]		[[Category: Four helix bundle]]
	[[Category: Helix loop helix]]		[[Category: Helix loop helix]]
-	[[Category: Nmr]]
	[[Category: Protein-peptide complex]]		[[Category: Protein-peptide complex]]
	[[Category: S100 protein]]		[[Category: S100 protein]]
	[[Category: S100b]]		[[Category: S100b]]
		+	[[Category: Structural protein]]
	[[Category: Trtk-12]]		[[Category: Trtk-12]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 02:44:36 2009''