title: The ever changing moods of calmodulin: how structural plasticity entails transductional adaptability.
abstract: The exceptional versatility of calmodulin (CaM) three-dimensional arrangement is reflected in the growing number of structural models of CaM/protein complexes currently available in the Protein Data Bank (PDB) database, revealing a great diversity of conformations, domain organization, and structural responses to Ca(2+). Understanding CaM binding is complicated by the diversity of target proteins sequences. Data mining of the structures shows that one face of each of the eight CaM helices can contribute to binding, with little overall difference between the Ca(2+) loaded N- and C-lobes and a clear prevalence of the C-lobe low Ca(2+) conditions. The structures reveal a remarkable variety of configurations where CaM binds its targets in a preferred orientation that can be reversed and where CaM rotates upon Ca(2+) binding, suggesting a highly dynamic metastable relation between CaM and its targets. Recent advances in structure-function studies and the discovery of CaM mutations being responsible for human diseases, besides expanding the role of CaM in human pathophysiology, are opening new exciting avenues for the understanding of the how CaM decodes Ca(2+)-dependent and Ca(2+)-independent signals.
authors.affiliation: Unidad de Biofísica, Consejo Superior de Investigaciones Científicas, CSIC-UPV/EHU, Barrio Sarriena s/n, 48940 Leioa, Spain. Electronic address: alvaro.villarroel@csic.es.
authors.forename: Alvaro
authors.initials: A
authors.lastname: Villarroel
authors.affiliation: Department of Medicine and Health Science, University of Molise, 86100 Campobasso, Italy. Electronic address: mtaglial@unina.it.
authors.forename: Maurizio
authors.initials: M
authors.lastname: Taglialatela
authors.affiliation: Unidad de Biofísica, Consejo Superior de Investigaciones Científicas, CSIC-UPV/EHU, Barrio Sarriena s/n, 48940 Leioa, Spain. Electronic address: ganeko7@gmail.com.
authors.forename: Ganeko
authors.initials: G
authors.lastname: Bernardo-Seisdedos
authors.affiliation: Unidad de Biofísica, Consejo Superior de Investigaciones Científicas, CSIC-UPV/EHU, Barrio Sarriena s/n, 48940 Leioa, Spain. Electronic address: alessalaimo@gmail.com.
authors.forename: Alessandro
authors.initials: A
authors.lastname: Alaimo
authors.affiliation: Unidad de Biofísica, Consejo Superior de Investigaciones Científicas, CSIC-UPV/EHU, Barrio Sarriena s/n, 48940 Leioa, Spain. Electronic address: jon.agirre@york.ac.uk.
authors.forename: Jon
authors.initials: J
authors.lastname: Agirre
authors.affiliation: Unidad de Biofísica, Consejo Superior de Investigaciones Científicas, CSIC-UPV/EHU, Barrio Sarriena s/n, 48940 Leioa, Spain. Electronic address: araitzalberdi@gmail.com.
authors.forename: Araitz
authors.initials: A
authors.lastname: Alberdi
authors.affiliation: Unidad de Biofísica, Consejo Superior de Investigaciones Científicas, CSIC-UPV/EHU, Barrio Sarriena s/n, 48940 Leioa, Spain. Electronic address: karolgomis@gmail.com.
authors.forename: Carolina
authors.initials: C
authors.lastname: Gomis-Perez
authors.affiliation: Department of Medicine and Health Science, University of Molise, 86100 Campobasso, Italy. Electronic address: mariavirginia.soldovieri@unimol.it.
authors.forename: Maria Virginia
authors.initials: MV
authors.lastname: Soldovieri
authors.affiliation: Department of Medicine and Health Science, University of Molise, 86100 Campobasso, Italy. Electronic address: paolo.ambrosino@unimol.it.
authors.forename: Paolo
authors.initials: P
authors.lastname: Ambrosino
authors.affiliation: Unidad de Biofísica, Consejo Superior de Investigaciones Científicas, CSIC-UPV/EHU, Barrio Sarriena s/n, 48940 Leioa, Spain. Electronic address: covadonga.m@gmail.com.
authors.forename: Covadonga
authors.initials: C
authors.lastname: Malo
authors.affiliation: Departamento de Farmacología, UPV/EHU, Universidad del País Vasco, Barrio Sarriena s/n, 48940 Leioa, Spain. Electronic address: pilar.areso@ehu.es.
authors.forename: Pilar
authors.initials: P
authors.lastname: Areso
mesh_terms: D000818:Animals; D020013:Calcium Signaling; D002147:Calmodulin / Q000737:chemistry* / Q000502:physiology*; D006801:Humans; D008958:Models, Molecular
chemical_list: D002147:Calmodulin
keywords: calcium; calmodulin; signal transduction