By Linda J. Van Eldik, D. Martin Watterson

ISBN-10: 0080926363

ISBN-13: 9780080926360

ISBN-10: 0127138609

ISBN-13: 9780127138602

This publication makes a speciality of rising topics 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 versions of cellphone 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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1993). The precise mechanism of regulation of this class of proteins is not fully understood, but it is believed to be similar to the regulatory mechanism used by the kinases and phosphatases (Crivici and Ikura, 1995). Even less is known about the role of calmodulin in the regulation of cytoskeletal proteins and their regulatory proteins. , 1990; Swanljung-Collins and Collins, 1991). The functional relevance of calmodulin interaction with these proteins is not clear. Because of the multidomain nature and large size of the target proteins of calmodulin, there is currently no three-dimensional structure determined for a complex between Ca 2 +-loaded calmodulin and any of its protein targets.

Disposition of methionine residues in the calcium-loaded state of calmodulin. The space-filling model of Ca 2 +-Ioaded calmodulin with methionine residues shaded in dark gray was rendered in Insight (MSI, San Diego, CA) using PDB coordinates lCLL. Two orientations are provided to visualize all of the methionines in the N-terminal and C-terminal domains. 2. Calmodulin as a Calcium Sensor 41 42 Melanie R. Nelson and Walter J. Chazin bon. This leads to stronger van der Waals contacts and also gives methionine a more plastic nature (Gellman, 1991), presumably allowing it to adapt to both sequestered and solvent accessible environments.

These peptides bound calmodulin with K d values of 10- 9 to 10- 10 M, which is in the range of the K d values seen for calmodulin target peptides. , 1992). When not bound to calmodulin, the peptide exchanges rapidly between the unfolded state and a helical conformation, which is populated a significant percentage of the time. When the peptide binds to calmodulin, it adopts a stable, helical conformation. , 1994). Presumably, these D analogs can make nonspecific van der Waals interactions with calmodulin, but will be unable to make the same specific hydrogen bonding and electrostatic interactions.

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

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