2b1u

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(New page: 200px<br /> <applet load="2b1u" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b1u" /> '''Solution structure of Calmodulin-like Skin ...)
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[[Image:2b1u.gif|left|200px]]<br />
 
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<applet load="2b1u" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2b1u" />
 
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'''Solution structure of Calmodulin-like Skin Protein C terminal domain'''<br />
 
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==Overview==
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==Solution structure of Calmodulin-like Skin Protein C terminal domain==
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The structure and dynamics of human calmodulin-like skin protein (CLSP), have been characterized by NMR spectroscopy. The mobility of CLSP has been, found to be different for the N-terminal and C-terminal domains. The, isolated domains were also expressed and analyzed. The structure of the, isolated C-terminal domain is presented. The N-terminal domain is, characterized by four stable helices, which experience large fluctuations., This is shown to be due to mutations in the hydrophobic core. The overall, N-terminal domain behavior is similar both in the full-length protein and, in the isolated domain. By exploiting the capability of Tb3+ bound to CLSP, to induce partial orientation of the molecule in a magnetic field, restricted motion of one domain with respect to the other was proved. By, using NMR, ITC, and ESI-MS, the calcium and magnesium binding properties, were investigated. Finally, CLSP is framed into the evolutionary scheme of, the calmodulin-like family.
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<StructureSection load='2b1u' size='340' side='right'caption='[[2b1u]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2b1u]] is a 1 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=2B1U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B1U FirstGlance]. <br>
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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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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2b1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b1u OCA], [https://pdbe.org/2b1u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b1u RCSB], [https://www.ebi.ac.uk/pdbsum/2b1u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b1u ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CALL5_HUMAN CALL5_HUMAN] Binds calcium. May be involved in terminal differentiation of keratinocytes.
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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/b1/2b1u_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=2b1u 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 structure and dynamics of human calmodulin-like skin protein (CLSP) have been characterized by NMR spectroscopy. The mobility of CLSP has been found to be different for the N-terminal and C-terminal domains. The isolated domains were also expressed and analyzed. The structure of the isolated C-terminal domain is presented. The N-terminal domain is characterized by four stable helices, which experience large fluctuations. This is shown to be due to mutations in the hydrophobic core. The overall N-terminal domain behavior is similar both in the full-length protein and in the isolated domain. By exploiting the capability of Tb3+ bound to CLSP to induce partial orientation of the molecule in a magnetic field, restricted motion of one domain with respect to the other was proved. By using NMR, ITC, and ESI-MS, the calcium and magnesium binding properties were investigated. Finally, CLSP is framed into the evolutionary scheme of the calmodulin-like family.
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==About this Structure==
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A structural and dynamic characterization of the EF-hand protein CLSP.,Babini E, Bertini I, Capozzi F, Chirivino E, Luchinat C Structure. 2006 Jun;14(6):1029-38. PMID:16765896<ref>PMID:16765896</ref>
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2B1U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2B1U OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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A structural and dynamic characterization of the EF-hand protein CLSP., Babini E, Bertini I, Capozzi F, Chirivino E, Luchinat C, Structure. 2006 Jun;14(6):1029-38. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16765896 16765896]
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</div>
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<div class="pdbe-citations 2b1u" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[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: Babini, E.]]
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[[Category: Babini E]]
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[[Category: Bertini, I.]]
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[[Category: Bertini I]]
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[[Category: Capozzi, F.]]
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[[Category: Capozzi F]]
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[[Category: Chirivino, E.]]
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[[Category: Chirivino E]]
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[[Category: Luchinat, C.]]
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[[Category: Luchinat C]]
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[[Category: SPINE, Structural.Proteomics.in.Europe.]]
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[[Category: backbone dynamic]]
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[[Category: calmodulin-like skin protein]]
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[[Category: clsp]]
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[[Category: nmr]]
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[[Category: solution structure]]
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[[Category: spine]]
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[[Category: structural genomics]]
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[[Category: structural proteomics in europe]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:57:10 2007''
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Current revision

Solution structure of Calmodulin-like Skin Protein C terminal domain

PDB ID 2b1u

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