Sandbox 213: Difference between revisions

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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.

CaM kinases have a catalytic N-terminal domain, a regulator domain, and a domain of association. The enzymes give an holoenzyme of dodecaméric 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 ~~autophosphoryltaed~~ one by one at the level of the thréonine residues 286.

CaM kinases have a catalytic N-terminal domain, a regulator domain, and a domain of association. The enzymes give an holoenzyme of dodecaméric 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 thréonine residues 286.

=Family members=

Sandbox 213: Difference between revisions

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@@ Line 76: / Line 76: @@
 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.
-CaM kinases have a catalytic N-terminal domain, a regulator domain, and a domain of association. The enzymes give an holoenzyme of dodecaméric 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 autophosphoryltaed one by one at the level of the thréonine residues  286.
+CaM kinases have a catalytic N-terminal domain, a regulator domain, and a domain of association. The enzymes give an holoenzyme of dodecaméric 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 thréonine residues  286.
 =Family members=