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Stefan2008 - calmodulin allostery


ABSTRACT: Stefan2008 - calmodulin allostery 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. This model is described in the article: An allosteric model of calmodulin explains differential activation of PP2B and CaMKII. Stefan MI, Edelstein SJ, Le Novère N Proc. Natl. Acad. Sci. U.S.A. 2008 Aug; 105(31): 10768-10773 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. This model is hosted on BioModels Database and identified by: BIOMD0000000183. To cite BioModels Database, please use: BioModels Database: An enhanced, curated and annotated resource for published quantitative kinetic models. To the extent possible under law, all copyright and related or neighbouring rights to this encoded model have been dedicated to the public domain worldwide. Please refer to CC0 Public Domain Dedication for more information.

SUBMITTER: Melanie Stefan  

PROVIDER: BIOMD0000000183 | BioModels | 2008-07-15

REPOSITORIES: BioModels

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Publications

An allosteric model of calmodulin explains differential activation of PP2B and CaMKII.

Stefan Melanie I MI   Edelstein Stuart J SJ   Le Novère Nicolas N  

Proceedings of the National Academy of Sciences of the United States of America 20080731 31


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  ...[more]

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