1uwo

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[[Image:1uwo.jpg|left|200px]]
 
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{{Structure
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==CALCIUM FORM OF HUMAN S100B, NMR, 20 STRUCTURES==
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|PDB= 1uwo |SIZE=350|CAPTION= <scene name='initialview01'>1uwo</scene>
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<StructureSection load='1uwo' size='340' side='right'caption='[[1uwo]]' scene=''>
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|SITE= <scene name='pdbsite=CA1:Pseudo+Ef-Hand+Ca-Binding+Site+Monomer+A'>CA1</scene>, <scene name='pdbsite=CA2:Canonical+Ef-Hand+Ca-Binding+Site+Monomer+A'>CA2</scene>, <scene name='pdbsite=CA3:Pseudo+Ef-Hand+Ca-Binding+Site+Monomer+B'>CA3</scene> and <scene name='pdbsite=CA4:Canonical+Ef-Hand+Ca-Binding+Site+Monomer+B'>CA4</scene>
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1uwo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UWO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UWO 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=
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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=1uwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uwo OCA], [https://pdbe.org/1uwo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uwo RCSB], [https://www.ebi.ac.uk/pdbsum/1uwo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uwo 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=1uwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uwo OCA], [http://www.ebi.ac.uk/pdbsum/1uwo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1uwo RCSB]</span>
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[https://www.uniprot.org/uniprot/S100B_HUMAN S100B_HUMAN] 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 (By similarity). Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization.<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/uw/1uwo_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=1uwo 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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BACKGROUND: S100B is a homodimeric member of the EF-hand calcium-binding protein superfamily. The protein has been implicated in cellular processes such as cell differentiation and growth, plays a role in cytoskeletal structure and function, and may have a role in neuropathological diseases, such as Alzheimers. The effects of S100B are mediated via its interaction with target proteins. While several studies have suggested that this interaction is propagated through a calcium-induced conformational change, leading to the exposure of a hydrophobic region of S100B, the molecular details behind this structural alteration remain unclear. RESULTS: The solution structure of calcium-saturated human S100B (Ca(2+)-S100B) has been determined by heteronuclear NMR spectroscopy. Ca(2+)-S100B forms a well defined globular structure comprising four EF-hand calcium-binding sites and an extensive hydrophobic dimer interface. A comparison of Ca(2+)-S100B with apo S100B and Ca(2+)-calbindin D9k indicates that while calcium-binding to S100B results in little change in the site I EF-hand, it induces a backbone reorientation of the N terminus of the site II EF-hand. This reorientation leads to a dramatic change in the position of helix III relative to the other helices. CONCLUSIONS: The calcium-induced reorientation of calcium-binding site II results in the increased exposure of several hydrophobic residues in helix IV and the linker region. While following the general mechanism of calcium modulatory proteins, whereby a hydrophobic target site is exposed, the 'calcium switch' observed in S100B appears to be unique from that of other EF-hand proteins and may provide insights into target specificity among calcium modulatory proteins.
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'''CALCIUM FORM OF HUMAN S100B, NMR, 20 STRUCTURES'''
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A novel calcium-sensitive switch revealed by the structure of human S100B in the calcium-bound form.,Smith SP, Shaw GS Structure. 1998 Feb 15;6(2):211-22. PMID:9519411<ref>PMID:9519411</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 1uwo" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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BACKGROUND: S100B is a homodimeric member of the EF-hand calcium-binding protein superfamily. The protein has been implicated in cellular processes such as cell differentiation and growth, plays a role in cytoskeletal structure and function, and may have a role in neuropathological diseases, such as Alzheimers. The effects of S100B are mediated via its interaction with target proteins. While several studies have suggested that this interaction is propagated through a calcium-induced conformational change, leading to the exposure of a hydrophobic region of S100B, the molecular details behind this structural alteration remain unclear. RESULTS: The solution structure of calcium-saturated human S100B (Ca(2+)-S100B) has been determined by heteronuclear NMR spectroscopy. Ca(2+)-S100B forms a well defined globular structure comprising four EF-hand calcium-binding sites and an extensive hydrophobic dimer interface. A comparison of Ca(2+)-S100B with apo S100B and Ca(2+)-calbindin D9k indicates that while calcium-binding to S100B results in little change in the site I EF-hand, it induces a backbone reorientation of the N terminus of the site II EF-hand. This reorientation leads to a dramatic change in the position of helix III relative to the other helices. CONCLUSIONS: The calcium-induced reorientation of calcium-binding site II results in the increased exposure of several hydrophobic residues in helix IV and the linker region. While following the general mechanism of calcium modulatory proteins, whereby a hydrophobic target site is exposed, the 'calcium switch' observed in S100B appears to be unique from that of other EF-hand proteins and may provide insights into target specificity among calcium modulatory proteins.
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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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1UWO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UWO OCA].
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__TOC__
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</StructureSection>
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==Reference==
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A novel calcium-sensitive switch revealed by the structure of human S100B in the calcium-bound form., Smith SP, Shaw GS, Structure. 1998 Feb 15;6(2):211-22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9519411 9519411]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Shaw, G S.]]
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[[Category: Shaw GS]]
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[[Category: Smith, S P.]]
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[[Category: Smith SP]]
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[[Category: calcium-binding protein]]
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[[Category: conformational change]]
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[[Category: ef-hand]]
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[[Category: human s100b]]
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[[Category: nmr]]
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[[Category: solution structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:16:20 2008''
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Current revision

CALCIUM FORM OF HUMAN S100B, NMR, 20 STRUCTURES

PDB ID 1uwo

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