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Deconvolution of Calcium-Binding Curves: Facts and Fantasies
Abstract
Ca2+signaling is of paramount importance in intracellular communication of eukaryotic cells. Many external stimuli trigger a transient change in the cytosolic-free Ca2+concentration (in the form of a Ca2+wave or Ca2+oscillations). The internal Ca2+modulation is deciphered by Ca2+-binding proteins, which undergo conformational changes upon Ca2+-binding allowing them to act as enzymatic or protein modulators. These Ca2+-binding proteins have been well described in the past three decades (16). Calmodulin, an ubiquitous and multifunctional protein, is considered as the prototype of the Ca2+-binding protein family containing EF-hand domains (716). Because of its pivotal role in many Ca2+-dependent cellular events, the understanding of the mechanism of action of this protein at the molecular level has been the aim of several research groups. For such a study, four main points have to be tackled:
–  Description of the mechanism of Ca2+-binding to calmodulin;
–  Understanding of the conformational changes induced by Ca2+-binding;
–  Analysis of the interaction of calmodulin with the different targets; and
–  Deciphering the activation or the modulation of the calmodulin/target protein complexes.
Affiliation(s): (2) Pharmacologie et Physico-Chimie des Interactions Cellulaires et Moléculaires, Faculté de Pharmacie, Université Louis Pasteur, Strasbourg, Illkirch, France
Series: Methods in Molecular Biology  |  Volume: 173  |  Pub. Date: Jan-24-2002  |  Page Range: 25-42  |  DOI: 10.1385/1-59259-184-1:025
Subject:  Protein Science
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