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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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