Calmodulin.

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Presentation transcript:

Calmodulin

Crystallographic structure of Calmodulin (CaM). Helix loop helix binding domains of CaM PDB ID 2L7L

asp glu

Cytosolic Ca+2 increases Role of Calmodulin. Stimulus Cytosolic Ca+2 increases Ca+2 binds to CaM and in turns binds to target proteins and activates it Reference: Michael. P. Walsh., Calmodulin and its roles in skeletal muscle function, 1983, 390-398.

Central linker region Pdb ID: 2L7L.

Blue-calcium ions bound to the active sites. Grey- alpha helices Blue-calcium ions bound to the active sites. And the ball and stick model of aspartates and glutamates which binds to the calcium ion. Pdb ID: 2L7L.

Oxygen atoms (carboxyl group) of aspartate and glutamate side chain binding to calcium ions. Pdb ID:2L7L.

Methionine residues which are responsible for binding to the target protein. Pdb id: 2L7L. Reference: Tao yuan., Hans.J.,Vogel. 1999. Substitution of methionine residues of calmodulin with the unnatural amino acid analogs ehionine and norleucine:Biochemical and specroscopic studies. Protein Science. 113-121.

Calmodulin-dependent enzymes. Role of Calmodulin. Calmodulin-dependent enzymes. Physiological role Cyclic nucleotide phosphodiesterase, Adenylate cyclase. Cyclic nucleotide metabolism. (Ca+2-Mg+2) ATPases. Myosin light chain kinase. Ca+2 transport Smooth muscle contraction and non-muscle motility. Phosphorylase kinase Glycogen metabolism. Reference: Michael. P. Walsh., Calmodulin and its roles in skeletal muscle function, 1983, 390-398.

Target protein myosin light chain kinase activated by the CaM showing the signalling pathway. Reference: Michael. P. Walsh., Calmodulin and its roles in skeletal muscle function, 1983, 390-398.

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