2b1u
From Proteopedia
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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
Page seeded by OCA on Thu Feb 21 16:33:22 2008
Categories: Homo sapiens | Single protein | Babini, E. | Bertini, I. | Capozzi, F. | Chirivino, E. | Luchinat, C. | SPINE, Structural Proteomics in Europe. | Backbone dynamic | Calmodulin-like skin protein | Clsp | Nmr | Solution structure | Spine | Structural genomics | Structural proteomics in europe
