Sandbox 213: Difference between revisions

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Charlene Planchenault

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 Calmodulin plays an important role through kinase enzymes such as calcium/calmodulin-dependent kinase II (CaMKII) that is a multifunctional serine/threonine kinase found in many tissues. Activation of CaMKII contributes to synaptic plasticity and regulation of excitory synaptic transmission. The regulatory domain of CaMKII contains an autophosphorylation site, which is essential for its calcium-dependent activation <ref name="Evans TI, Shea MA. Energetics of calmodulin domain interactions with the calmodulin binding domain of CaMKII. Proteins. 2009 Jul;76(1):47-61. PMID:19089983. doi :[[10.1002/prot.22317]]"/>.
-CaM kinases have a catalytic N-terminal domain, a regulator domain and an association domain. The enzymes give an holoenzyme of dodecameric structure, the catalytics domains are found one's way out side, that permit of phosphorylate the residues between the sub-unit. Without Ca2+/calmodulin, the catalytic domain is self-inhibited by the regulator domain, which contains one sequence of type pseudo-substrate. Many CaM kinases give an homo-oligomeres or hetero-oligomeres. When there is an activation by the Ca2+/calmodulin complex, the CaM kinases actif are autophosphorylated one by one at the level of the threonine residues  286.
+CaM kinases have a catalytic N-terminal domain, a regulator domain and a domain of association. Many CaM form an holoenzyme with a dodecameric structure(the catalytics domains are found one's way out side) that permit to phosphorylate the residues between the sub-unit. Without Ca2+/calmodulin, the catalytic domain is self-inhibited by the regulator domain, which contains one sequence of type pseudo-substrate. Many CaM kinases give an homo-oligomeres or hetero-oligomeres. When there is an activation by the Ca2+/calmodulin complex, the actif CaM kinases are autophosphorylated one by one at the level of the threonine 286 residues.
 =Family members=