By Linda J. Van Eldik, D. Martin Watterson
This publication specializes in rising subject matters 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 telephone legislation via calmodulin-regulated pathways and their linkage with different regulatory pathways. Highlights: * Molecular mechanisms of calcium sign transduction through calmodulin-regulated enzymes * chosen case reports and precedents on the topic of molecular mechanisms * Protein-protein acceptance among calmodulin and the enzymes it regulates * Cross-talk and interdigitation with different sign transduction pathways. Read more...
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Additional resources for Calmodulin and Signal Transduction
1984). Not only does the single TFP molecule in the Cook et al. (1994) structures bind to the C-terminal domain, but in the structure with four TFP molecules bound, the TFP molecule in the C-terminal pocket has the best density of the four molecules. Interestingly, the TFP molecule with the poorest density is bound in the hydrophobic pocket of the N-terminal domain. The remaining two TFP molecules are bound to other parts of the hydrophobic "tunnel" created by the hydrophobic pockets of the two domains.
This causes the trifluoromethyl group and the piperazine ring to point in opposite directions in the two structures. , 1984). Not only does the single TFP molecule in the Cook et al. (1994) structures bind to the C-terminal domain, but in the structure with four TFP molecules bound, the TFP molecule in the C-terminal pocket has the best density of the four molecules. Interestingly, the TFP molecule with the poorest density is bound in the hydrophobic pocket of the N-terminal domain. The remaining two TFP molecules are bound to other parts of the hydrophobic "tunnel" created by the hydrophobic pockets of the two domains.
13. Interactions between the conserved arginine from the tar get peptide and the calmodulin linker region. Arginine-812 from the MLCK peptide hydrogen bond s with two residu es of calmodulin at the beginning and at the end of the flexible teth er betwe en the N-terminal and the C-terminal domains. This arginine, found one residue befor e the Cterminal hydrophobic anchor of the peptide , is well conserved in calmodulin tar get peptides. Calmodulin is light gray and the MLCK peptide is dark gray.