Ontology highlight
ABSTRACT:
SUBMITTER: Stefan MI
PROVIDER: S-EPMC2504824 | biostudies-literature | 2008 Aug
REPOSITORIES: biostudies-literature
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]