2b1u

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[[Image:2b1u.gif|left|200px]]
[[Image:2b1u.gif|left|200px]]
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{{Structure
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|GENE= CALML5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|RESOURCES=<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://www.ebi.ac.uk/pdbsum/2b1u PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2b1u RCSB]</span>
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'''Solution structure of Calmodulin-like Skin Protein C terminal domain'''
'''Solution structure of Calmodulin-like Skin Protein C terminal domain'''
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[[Category: Luchinat, C.]]
[[Category: Luchinat, C.]]
[[Category: SPINE, Structural Proteomics in Europe.]]
[[Category: SPINE, Structural Proteomics in Europe.]]
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[[Category: backbone dynamic]]
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[[Category: Backbone dynamic]]
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[[Category: calmodulin-like skin protein]]
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[[Category: Calmodulin-like skin protein]]
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[[Category: clsp]]
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[[Category: Clsp]]
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[[Category: nmr]]
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[[Category: Nmr]]
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[[Category: solution structure]]
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[[Category: Solution structure]]
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[[Category: spine]]
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[[Category: Spine]]
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[[Category: structural genomic]]
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[[Category: Structural genomic]]
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[[Category: structural proteomics in europe]]
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[[Category: Structural proteomics in europe]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:17:19 2008''
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Revision as of 05:17, 13 April 2008

Template:STRUCTURE 2b1u

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 Sun Apr 13 08:17:19 2008

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