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.

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="Fallon JL, Quiocho FA. A closed compact structure of native Ca(2+)-calmodulin. Structure. 2003 Oct;11(10):1303-7. PMID :[[14527397]]"/>.

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.

Sandbox 213: Difference between revisions

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Revision as of 15:09, 2 January 2012 view source Charlene Planchenault (talk \| contribs) 257 edits No edit summary ← Older edit		Revision as of 15:10, 2 January 2012 view source Charlene Planchenault (talk \| contribs) 257 edits No edit summary Newer edit →
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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.		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="Fallon JL, Quiocho FA. A closed compact structure of native Ca(2+)-calmodulin. Structure. 2003 Oct;11(10):1303-7. PMID :[[14527397]]"/>.


	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 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.