Sandbox 213: Difference between revisions
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'''Calmodulin''' [http://www.rcsb.org/pdb/101/motm_disscussed_entry.do?id=3cln] | '''Calmodulin''' [http://www.rcsb.org/pdb/101/motm_disscussed_entry.do?id=3cln] | ||
[[Image:calmodulin_Ca_site.gif|right|200px]] | |||
Calmodulin contains four Ca<sup>2+</sup> binding sites and the binding of calcium induces a conformational change in calmodulin that can cause the activation of key enzymes such as kinases or phosphatases proteins (especially phosphorylase kinases) which are not necessarily themselves Ca<sup>2+</sup>-sensitive and allows a large diversity of cellular response. | Calmodulin contains four Ca<sup>2+</sup> binding sites and the binding of calcium induces a conformational change in calmodulin that can cause the activation of key enzymes such as kinases or phosphatases proteins (especially phosphorylase kinases) which are not necessarily themselves Ca<sup>2+</sup>-sensitive and allows a large diversity of cellular response. | ||
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The two EF-hands are located in the vicinity of each other. Those neighboring sited are very likely to structurally influence each other upon Ca<sup>2+</sup> binding to one of them. | The two EF-hands are located in the vicinity of each other. Those neighboring sited are very likely to structurally influence each other upon Ca<sup>2+</sup> binding to one of them. | ||
A superfamily of proteins utilizes the configuration of helix-loop-helix to bind Ca<sup>2+</sup> but calmodulin is the only member that subserves so many functions. | A superfamily of proteins utilizes the configuration of helix-loop-helix to bind Ca<sup>2+</sup> but calmodulin is the only member that subserves so many functions. | ||
