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. 1995 Oct 16;14(20):4922–4931. doi: 10.1002/j.1460-2075.1995.tb00175.x

Molecular mechanism of the calcium-induced conformational change in the spectrin EF-hands.

G Travé 1, P J Lacombe 1, M Pfuhl 1, M Saraste 1, A Pastore 1
PMCID: PMC394594  PMID: 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.

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