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Solution structure of Calmodulin-like Skin Protein C terminal domainSolution structure of Calmodulin-like Skin Protein C terminal domain
Structural highlights
FunctionCALL5_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 PubMedThe 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
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