1b4c

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[[Image:1b4c.jpg|left|200px]]
 
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{{Structure
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==SOLUTION STRUCTURE OF RAT APO-S100B USING DIPOLAR COUPLINGS==
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|PDB= 1b4c |SIZE=350|CAPTION= <scene name='initialview01'>1b4c</scene>
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<StructureSection load='1b4c' size='340' side='right'caption='[[1b4c]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1b4c]] 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=1B4C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B4C FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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|GENE= S100BETA FROM RATTUS NORVEGICUS (RAT) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1b4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b4c OCA], [https://pdbe.org/1b4c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b4c RCSB], [https://www.ebi.ac.uk/pdbsum/1b4c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b4c ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b4c OCA], [http://www.ebi.ac.uk/pdbsum/1b4c PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b4c RCSB]</span>
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[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>
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b4/1b4c_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1b4c ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The relative orientations of adjacent structural elements without many well-defined NOE contacts between them are typically poorly defined in NMR structures. For apo-S100B(betabeta) and the structurally homologous protein calcyclin, the solution structures determined by conventional NMR exhibited considerable differences and made it impossible to draw unambiguous conclusions regarding the Ca2+-induced conformational change required for target protein binding. The structure of rat apo-S100B(betabeta) was recalculated using a large number of constraints derived from dipolar couplings that were measured in a dilute liquid crystalline phase. The dipolar couplings orient bond vectors relative to a single-axis system, and thereby remove much of the uncertainty in NOE-based structures. The structure of apo-S100B(betabeta) indicates a minimal change in the first, pseudo-EF-hand Ca2+ binding site, but a large reorientation of helix 3 in the second, classical EF-hand upon Ca2+ binding.
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'''SOLUTION STRUCTURE OF RAT APO-S100B USING DIPOLAR COUPLINGS'''
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The use of dipolar couplings for determining the solution structure of rat apo-S100B(betabeta).,Drohat AC, Tjandra N, Baldisseri DM, Weber DJ Protein Sci. 1999 Apr;8(4):800-9. PMID:10211826<ref>PMID:10211826</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1b4c" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The relative orientations of adjacent structural elements without many well-defined NOE contacts between them are typically poorly defined in NMR structures. For apo-S100B(betabeta) and the structurally homologous protein calcyclin, the solution structures determined by conventional NMR exhibited considerable differences and made it impossible to draw unambiguous conclusions regarding the Ca2+-induced conformational change required for target protein binding. The structure of rat apo-S100B(betabeta) was recalculated using a large number of constraints derived from dipolar couplings that were measured in a dilute liquid crystalline phase. The dipolar couplings orient bond vectors relative to a single-axis system, and thereby remove much of the uncertainty in NOE-based structures. The structure of apo-S100B(betabeta) indicates a minimal change in the first, pseudo-EF-hand Ca2+ binding site, but a large reorientation of helix 3 in the second, classical EF-hand upon Ca2+ binding.
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*[[S100 proteins 3D structures|S100 proteins 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1B4C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B4C OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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The use of dipolar couplings for determining the solution structure of rat apo-S100B(betabeta)., Drohat AC, Tjandra N, Baldisseri DM, Weber DJ, Protein Sci. 1999 Apr;8(4):800-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10211826 10211826]
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Baldisseri DM]]
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[[Category: Baldisseri, D M.]]
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[[Category: Drohat AC]]
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[[Category: Drohat, A C.]]
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[[Category: Tjandra N]]
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[[Category: Tjandra, N.]]
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[[Category: Weber DJ]]
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[[Category: Weber, D J.]]
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[[Category: calcium- binding protein]]
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[[Category: dipolar coupling]]
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[[Category: ef-hand]]
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[[Category: four-helix bundle]]
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[[Category: nmr]]
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[[Category: s100 protein]]
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[[Category: s100b]]
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[[Category: s100beta]]
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[[Category: solution structure]]
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[[Category: three-dimensional structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:53:19 2008''
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Current revision

SOLUTION STRUCTURE OF RAT APO-S100B USING DIPOLAR COUPLINGS

PDB ID 1b4c

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