Molecular mechanism of the calcium-induced conformational change in the spectrin EF-hands
| Autor: | Pj Lacombe, Matti Saraste, Annalisa Pastore, Mark Pfuhl, Gilles Travé |
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| Přispěvatelé: | Centre National de la Recherche Scientifique (CNRS), Trave, G, Lacombe, Pj, Pfuhl, M, Saraste, M, Pastore, A |
| Jazyk: | angličtina |
| Rok vydání: | 1995 |
| Předmět: |
Models
Molecular Conformational change Magnetic Resonance Spectroscopy Calmodulin Protein Conformation MESH: Sequence Homology Amino Acid [SDV]Life Sciences [q-bio] Molecular Sequence Data chemistry.chemical_element MESH: Amino Acid Sequence Biology Calcium MESH: Troponin C General Biochemistry Genetics and Molecular Biology Troponin C 03 medical and health sciences Protein structure MESH: Protein Conformation MESH: Computer Simulation Computer Simulation Spectrin Amino Acid Sequence Molecular Biology 030304 developmental biology 0303 health sciences MESH: Molecular Sequence Data Sequence Homology Amino Acid General Immunology and Microbiology MESH: Magnetic Resonance Spectroscopy General Neuroscience 030302 biochemistry & molecular biology MESH: Spectrin Troponin Cytosol chemistry Biochemistry MESH: Calcium Biophysics biology.protein MESH: Troponin Signal transduction MESH: Models Molecular Research Article |
| Zdroj: | EMBO Journal EMBO Journal, EMBO Press, 1995, 14 (20), pp.4922-31 Europe PubMed Central |
| ISSN: | 0261-4189 1460-2075 |
| Popis: | International audience; Calcium is a universally employed cytosolic messenger in eukaryotic cells. Most of the proteins that bind signalling calcium are members of the calmodulin superfamily and share two or more helix-loop-helix motifs known as EF-hands. A model, based on structure comparison of different domains and supported by preliminary NMR data, has suggested that EF-hands involved in signal transduction undergo a major conformational change upon calcium binding from a 'closed' to an 'open' state allowing protein-protein interaction. We have determined the solution structures of the EF-hand pair from alpha-spectrin in the absence and in the presence of calcium. The structures are in the closed and open conformation respectively, providing a definite experimental proof for the closed-to-open model. Our results allow formulation of the rules which govern the movement induced by calcium. These rules may be generalized to other EF-hands since the key residues involved are conserved within the calmodulin family. |
| Databáze: | OpenAIRE |
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