Stefan2008 - calmodulin allostery
View the 2009-03 Model of the Month entry for this modelAn allosteric model for calmodulin activation, in which binding to calcium facilitates the transition between a low-affinity [tense (T)] and a high-affinity [relaxed (R)] state.
This model is described in the article:
Abstract:
Calmodulin plays a vital role in mediating bidirectional synaptic plasticity by activating either calcium/calmodulin-dependent protein kinase II (CaMKII) or protein phosphatase 2B (PP2B) at different calcium concentrations. We propose an allosteric model for calmodulin activation, in which binding to calcium facilitates the transition between a low-affinity [tense (T)] and a high-affinity [relaxed (R)] state. The four calcium-binding sites are assumed to be nonidentical. The model is consistent with previously reported experimental data for calcium binding to calmodulin. It also accounts for known properties of calmodulin that have been difficult to model so far, including the activity of nonsaturated forms of calmodulin (we predict the existence of open conformations in the absence of calcium), an increase in calcium affinity once calmodulin is bound to a target, and the differential activation of CaMKII and PP2B depending on calcium concentration.
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An allosteric model of calmodulin explains differential activation of PP2B and CaMKII.
- Melanie I Stefan, Stuart J Edelstein, Nicolas Le Novère
- Proceedings of the National Academy of Sciences of the United States of America , 8/ 2008 , Volume 105 , Issue 31 , pages: 10768-10773 , PubMed ID: 18669651
Submitter of this revision: Lucian Smith
Curator: Lucian Smith
Modeller: Melanie Stefan
Metadata information
isDescribedBy (1 statement)
hasTaxon (1 statement)
isVersionOf (5 statements)
Gene Ontology protein serine/threonine phosphatase activity
Gene Ontology detection of calcium ion
Gene Ontology calmodulin binding
Gene Ontology positive regulation of synaptic plasticity
isPartOf (2 statements)
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