2b1u

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Revision as of 18:50, 12 November 2007

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Solution structure of Calmodulin-like Skin Protein C terminal domain

Overview

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.

About this Structure

2B1U is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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

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