2B1U

Solution structure of Calmodulin-like Skin Protein C terminal domain

Summary for 2B1U

• Entry DOI: 10.2210/pdb2b1u/pdb
• NMR Information: BMRB: 6841
• Descriptor: Calmodulin-like protein 5 (1 entity in total)
• Functional Keywords: clsp, calmodulin-like skin protein, solution structure, backbone dynamic, structural genomics, structural proteomics in europe, spine, metal binding protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 7969.74

Authors

Babini, E.,Bertini, I.,Capozzi, F.,Chirivino, E.,Luchinat, C.,Structural Proteomics in Europe (SPINE) (deposition date: 2005-09-16, release date: 2006-05-30, Last modification date: 2024-05-29)

Primary citation

Babini, E.,Bertini, I.,Capozzi, F.,Chirivino, E.,Luchinat, C.
A Structural and Dynamic Characterization of the EF-Hand Protein CLSP.
Structure, 14:1029-1038, 2006

PubMed Abstract: 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.

PubMed: 16765896
DOI: 10.1016/j.str.2006.04.004

Experimental method

SOLUTION NMR