Structural basis for the autoinhibition of calcium/calmodium-dependent protein kinase I

Article Abstract:

Calcium/calmodulin-dependent protein kinases (CaM kinases) play a active role in the regulation of diverse cellular processes. CaM kinases, which are activated by the calcium sensor calmodulin, influence such processes as cell proliferation, gene expression, muscle contraction and neurotransmitter release. The crystal structure of CaM kinase 1 in its autoinhibition form shows that calmodulin binds to the C-terminal regulatory region. This process, which leads to kinase activation, results in substantial structural changes in CaM kinase 1.

Enzymes, Proteins, Calmodulin, Enzyme regulation, Protein conformation, Calcium-binding proteins, Calcium binding proteins

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An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor

Article Abstract:

A study finds that the epidermal growth factor receptor (EGFR) kinase domain can be activated by increasing its local concentration or by mutating a leucine (L834R) in the activation loop, the phosphorylation of which is not required for activation. By this, it is suggested that the kinase domain is intrinsically auto-inhibited, and that an intermolecular interaction promotes its activation.

Epidermal growth factor receptors

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Structural analysis of autoinhibition in the Ras activator Son of sevenless

Article Abstract:

A crystallographic and biochemical analyses of a construct of Son of sevenless (SOS) that contains the Dbl homologypleckstrin homology (DH-PH) and catalytic domains is presented. It is observed that the DH-PH unit blocks the allosteric binding site for Ras and suppresses the activity of SOS.

Cells (Biology), Cells, Ras genes

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