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| | ==SOLUTION STRUCTURE OF RAT APO-S100B USING DIPOLAR COUPLINGS== | | ==SOLUTION STRUCTURE OF RAT APO-S100B USING DIPOLAR COUPLINGS== |
| - | <StructureSection load='1b4c' size='340' side='right'caption='[[1b4c]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''> | + | <StructureSection load='1b4c' size='340' side='right'caption='[[1b4c]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1b4c]] 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=1B4C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B4C FirstGlance]. <br> | + | <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> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">S100BETA FROM RATTUS NORVEGICUS (RAT) ([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=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> | | <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> |
| | </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]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Baldisseri, D M]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Drohat, A C]] | + | [[Category: Baldisseri DM]] |
| - | [[Category: Tjandra, N]] | + | [[Category: Drohat AC]] |
| - | [[Category: Weber, D J]] | + | [[Category: Tjandra N]] |
| - | [[Category: Calcium- binding protein]] | + | [[Category: Weber DJ]] |
| - | [[Category: Dipolar coupling]]
| + | |
| - | [[Category: Ef-hand]]
| + | |
| - | [[Category: Four-helix bundle]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| - | [[Category: S100 protein]]
| + | |
| - | [[Category: S100b]]
| + | |
| - | [[Category: S100beta]]
| + | |
| - | [[Category: Solution structure]]
| + | |
| - | [[Category: Three-dimensional structure]]
| + | |
| Structural highlights
Function
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.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tsoporis JN, Izhar S, Leong-Poi H, Desjardins JF, Huttunen HJ, Parker TG. S100B interaction with the receptor for advanced glycation end products (RAGE): a novel receptor-mediated mechanism for myocyte apoptosis postinfarction. Circ Res. 2010 Jan 8;106(1):93-101. doi: 10.1161/CIRCRESAHA.109.195834. Epub 2009, Nov 12. PMID:19910580 doi:10.1161/CIRCRESAHA.109.195834
- ↑ Gilquin B, Cannon BR, Hubstenberger A, Moulouel B, Falk E, Merle N, Assard N, Kieffer S, Rousseau D, Wilder PT, Weber DJ, Baudier J. The calcium-dependent interaction between S100B and the mitochondrial AAA ATPase ATAD3A and the role of this complex in the cytoplasmic processing of ATAD3A. Mol Cell Biol. 2010 Jun;30(11):2724-36. doi: 10.1128/MCB.01468-09. Epub 2010 Mar , 29. PMID:20351179 doi:10.1128/MCB.01468-09
- ↑ Drohat AC, Tjandra N, Baldisseri DM, Weber DJ. The use of dipolar couplings for determining the solution structure of rat apo-S100B(betabeta). Protein Sci. 1999 Apr;8(4):800-9. PMID:10211826
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