title: New aspects of calmodulin-calmodulin binding domains recognition.
abstract: Understanding the role of calmodulin (CaM) in calcium signal transduction implies to describe the -calcium-dependent molecular mechanism of interaction of CaM with the various CaM-binding domains (CBD). In order to fulfill this aim, we have developed a new strategy and the afferent techniques to quantify the interaction of CaM with any CBD as a function of calcium concentration. Excel software has been used to deconvolute the experimental data and to obtain the macroscopic constants characterizing the system. We are illustrating our approach on six different CaM/CBD. This strategy may be used to analyze the interaction between any calcium-binding protein and its targets.
authors.affiliation: Faculté de Pharmacie, Laboratoire d'Innovation Thérapeutique, URM 7200, Université de Strasbourg, F-Illkirch, France.
authors.forename: Emilie
authors.initials: E
authors.lastname: Audran
authors.forename: Rania
authors.initials: R
authors.lastname: Dagher
authors.forename: Sophie
authors.initials: S
authors.lastname: Gioria
authors.forename: Marie-Claude
authors.initials: MC
authors.lastname: Kilhoffer
authors.forename: Jacques
authors.initials: J
authors.lastname: Haiech
mesh_terms: D000595:Amino Acid Sequence; D002021:Buffers; D002147:Calmodulin / Q000737:chemistry* / Q000378:metabolism*; D005454:Fluorescence Polarization; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary
chemical_list: D002021:Buffers; D002147:Calmodulin; D010455:Peptides