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 ~~régulator~~ domain, and an association domain. The enzymes give an holoenzyme of structure dodécaméric, the catalytics domains are fond one's way ou side, that permit of phosphoryler the résidus between the sub-unit. Without Ca2+/calmodulin, the catalytic domain is auto-inhibé by the régulator domain , which contains one sequence of type pseudo-substrat. Many CaM kinases give an homo-oligomères or hétéro-oligomères. When there is an activation by the Ca2+/calmodulincomplexe , the CaM kinases actif are autophosphoryled one by one at the level of the thréonineresidue 286.

CaM kinases have a catalytic N-terminal domain, a regulator domain, and an association domain. The enzymes give an holoenzyme of structure dodécaméric, the catalytics domains are fond one's way out side, that permit of phosphoryler the résidus between the sub-unit. Without Ca2+/calmodulin, the catalytic domain is auto-inhibé by the régulator domain , which contains one sequence of type pseudo-substrat. Many CaM kinases give an homo-oligomères or hétéro-oligomères. When there is an activation by the Ca2+/calmodulincomplexe , the CaM kinases actif are autophosphoryled one by one at the level of the thréonineresidue 286.

=Family members=

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 régulator domain, and an association domain. The enzymes give an holoenzyme of structure dodécaméric, the catalytics domains are fond one's way ou side, that permit of phosphoryler the résidus between the sub-unit. Without Ca2+/calmodulin, the catalytic domain is auto-inhibé by the régulator domain , which contains one sequence of type pseudo-substrat. Many CaM kinases give an homo-oligomères or hétéro-oligomères. When there is an activation by the Ca2+/calmodulincomplexe , the CaM kinases actif are autophosphoryled one by one at the level of the thréonineresidue  286.
+CaM kinases have a catalytic N-terminal domain, a regulator domain, and an association domain. The enzymes give an holoenzyme of structure dodécaméric, the catalytics domains are fond one's way out side, that permit of phosphoryler the résidus between the sub-unit. Without Ca2+/calmodulin, the catalytic domain is auto-inhibé by the régulator domain , which contains one sequence of type pseudo-substrat. Many CaM kinases give an homo-oligomères or hétéro-oligomères. When there is an activation by the Ca2+/calmodulincomplexe , the CaM kinases actif are autophosphoryled one by one at the level of the thréonineresidue  286.
 =Family members=