Download e-book for kindle: Calmodulin and Signal Transduction by Linda J. Van Eldik, D. Martin Watterson

By Linda J. Van Eldik, D. Martin Watterson

ISBN-10: 0080926363

ISBN-13: 9780080926360

ISBN-10: 0127138609

ISBN-13: 9780127138602

This ebook specializes in rising issues within the molecular mechanisms of calcium sign transduction via calmodulin-regulated pathways. It offers the reader with chosen examples and experimental precedents that underlie present types of mobilephone rules 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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Example text

This nonspecificity may be further aided by the amino acid composition of the hydrophobic surface of calmodulin. The methionines, which constitute such a substantial portion of this hydrophobic interface, appear to have an important role to play, as all nine are found to interact with the peptide. Here again, the special features of the methionine side chain (the flexibility 50 Melanie R. Nelson and Walter J. Chazin and increased polarizability of the sulfur atom relative to carbon) make it an ideal residue for the strong, but nonspecific van der Waals interactions required for binding to the multitude of calmodulin receptors (O'Neil and DeGrado, 1990; Vogel and Zhang, 1995).

However, although NMR showed the calmodulin-LsmMLCK complex to be in slow exchange with its dissociated compo- 2. Calmodulin as a Calcium Sensor 53 nents tk;« --- 1 sec"), the calmodulin-D-smMLCK complex was in fast exchange tk;« --- 102 sec:'), indicative of weaker binding. , 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.

The general mode of binding of the peptide is also conserved. In all three structures, the peptide is engulfed in the interdomain hydrophobic channel, anchored at both ends by large hydrophobic residues from the peptide (Fig. 11). Thus, all three complexes are stabilized by extensive hydrophobic interactions. Electrostatic interactions are also seen between the basic residues found at the N terminus of the peptide and nearby acidic residues on calmodulin. Whereas the two structures of calmodulin-MLCK peptide complexes are extremely similar, there are some significant differences between them and the calmodulin-CaMKII peptide structure (Fig.

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

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