Calmodulin and Signal Transduction by Linda J. Van Eldik, D. Martin Watterson

By Linda J. Van Eldik, D. Martin Watterson

This booklet specializes in rising topics within the molecular mechanisms of calcium sign transduction via calmodulin-regulated pathways. It presents the reader with chosen examples and experimental precedents that underlie present types of mobilephone legislation via calmodulin-regulated pathways and their linkage with different regulatory pathways. Highlights: * Molecular mechanisms of calcium sign transduction through Read more...

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1990). Furthermore, NMR methods find two major binding sites for TFP on calmodulin, one in each domain, and localize these sites to the same region as used in peptide binding. , 1996). Even the two crystal structures of the calmodulin-TFP complexes do not clear up the confusion over the number of binding sites. , 1994). Both structures show a globular conformation of calmodulin very similar to that seen in calmodulin-peptide complexes. Both also have a TFP molecule bound in the hydrophobic pocket of the C-terminal domain, although the phenothiazine ring in one structure is rotated 180 with respect to its position in the other structure.

1994). The differences between the binding of the Dpeptide and the L peptide may be due to a difference between the formation of a complex based only on nonspecific van der Waals interactions and a more specific complex also involving the key hydrogen-bonding and electrostatic interactions seen in the three calmodulin-peptide structures. This interpretation is supported by kinetic data on the binding of sMLCK peptide to calmodulin. The binding event was shown to involve two steps: a fast association step and a slower isomerization step (Torok and Trentham, 1994).

There are many similarities among these three structures. The overall structure of calmodulin in all three complexes is globular and ellipsoid. The central helix connecting the two globular domains of calmodulin is disrupted in the bound structures, allowing the N-terminal and MLCK peptide 2. Calmodulin as a Calcium Sensor 45 C-terminal domains, which are quite far apart in the uncomplexed Ca 2 +loaded calmodulin structure, to come into close proximity with each other and even form contacts (Fig.

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