Molecular mechanism of the calcium-induced conformational change in the spectrin EF-hands.
EMBO J
; 14(20): 4922-31, 1995 Oct 16.
Article
en En
| MEDLINE
| ID: mdl-7588621
ABSTRACT
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.
Texto completo:
1
Base de datos:
MEDLINE
Asunto principal:
Calcio
/
Espectrina
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
EMBO J
Año:
1995
Tipo del documento:
Article