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| | ==Solution structure of Calmodulin-like Skin Protein C terminal domain== | | ==Solution structure of Calmodulin-like Skin Protein C terminal domain== |
| - | <StructureSection load='2b1u' size='340' side='right' caption='[[2b1u]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2b1u' size='340' side='right'caption='[[2b1u]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2b1u]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2B1U FirstGlance]. <br> | + | <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> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CALML5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b1u OCA], [http://pdbe.org/2b1u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2b1u RCSB], [http://www.ebi.ac.uk/pdbsum/2b1u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2b1u 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=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> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CALL5_HUMAN CALL5_HUMAN]] Binds calcium. May be involved in terminal differentiation of keratinocytes. | + | [https://www.uniprot.org/uniprot/CALL5_HUMAN CALL5_HUMAN] Binds calcium. May be involved in terminal differentiation of keratinocytes. |
| | == 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: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Babini, E]] | + | [[Category: Large Structures]] |
| - | [[Category: Bertini, I]] | + | [[Category: Babini E]] |
| - | [[Category: Capozzi, F]] | + | [[Category: Bertini I]] |
| - | [[Category: Chirivino, E]] | + | [[Category: Capozzi F]] |
| - | [[Category: Luchinat, C]] | + | [[Category: Chirivino E]] |
| - | [[Category: SPINE, Structural Proteomics in Europe]]
| + | [[Category: Luchinat C]] |
| - | [[Category: Backbone dynamic]]
| + | |
| - | [[Category: Calmodulin-like skin protein]]
| + | |
| - | [[Category: Clsp]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| - | [[Category: Solution structure]]
| + | |
| - | [[Category: Spine]]
| + | |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Structural proteomics in europe]]
| + | |
| Structural highlights
Function
CALL5_HUMAN Binds calcium. May be involved in terminal differentiation of keratinocytes.
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 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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Babini E, Bertini I, Capozzi F, Chirivino E, Luchinat C. A structural and dynamic characterization of the EF-hand protein CLSP. Structure. 2006 Jun;14(6):1029-38. PMID:16765896 doi:http://dx.doi.org/10.1016/j.str.2006.04.004
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