The cellular response to the second messenger is a mutation that affects ca++ binding to calmodulin and is most likely to interfere with what aspect of a signal transduction pathway.
<h3>Ca++ binding to calmodulin :</h3>
This protein-protein interaction ultimately has a physiological consequence; for instance, in smooth muscle, Ca2+ binding to calmodulin causes it to connect with and activate myosin light chain kinase, which in turn catalyzes the phosphorylation of myosin. The smooth muscle contracts as a result of this reaction.
A common, tiny (148 amino acids) calcium signaling protein called calmodulin (CaM) controls the actions of numerous cellular proteins. It has two calcium-binding sites in the N-domain (I and II) and two more in the C-domain (III and IV).
In order for smooth muscle to contract, calmodulin is crucial for excitation-contraction (EC) coupling and the start of the cross-bridge cycling in smooth muscle. The head of the myosin light chain must be phosphorylated to initiate smooth muscle contraction.
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