Molecular Mechanism of Target Recognition by Calmodulin

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9-1) Small-angle X-ray scattering (SAXS) was used to investigate the conformational changes of calmodulin on binding to a calmodulin-binding sequence in myosin light chain kinase, calcineurin, calmodulin-protein kinase. I, II, IV and these binding motifs were determined on the molecular level.9-2) SAXS was used to investigate the conformational changes of calmodulin on binding to a myristoylated N-terminal nonapeptide from neuron-specific protein CAP-23/NAP-22 and the binding motif was determined on the molecular level.9-3) SAXS was used to investigate the conformational changes of calmodulin on binding to an antagonist like W-7 and TFP and the binding motif was determined on the molecular level.9-4) In the absence of Ca^<2+>, a new binding motif was found in the calmodulin/TFP and calmodulin/calmodulin-dependent protein kinase TV complexes.9-5) SAXS was used to reveal the role of the central helix in calmodulin for its recognition.9-6) SAXS with stopped-flow technique was used to reveal the kinetic conformational change of Ca^<2+>-dependent target recognition by calmodulin.