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Calmodulin
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Crystallographic structure of Calmodulin (CaM).
Helix loop helix binding domains of CaM PDB ID 2L7L
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asp glu
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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,
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Central linker region Pdb ID: 2L7L.
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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.
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Oxygen atoms (carboxyl group) of aspartate and glutamate side chain binding to calcium ions.
Pdb ID:2L7L.
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Methionine residues which are responsible for binding to the target protein.
Pdb id: 2L7L. Reference: Tao yuan., Hans.J.,Vogel Substitution of methionine residues of calmodulin with the unnatural amino acid analogs ehionine and norleucine:Biochemical and specroscopic studies. Protein Science
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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,
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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,
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