title: Structural diversity of calmodulin binding to its target sites.
abstract: Calmodulin (CaM) is a ubiquitous, highly conserved, eukaryotic protein that binds to and regulates a number of diverse target proteins involved in different functions such as metabolism, muscle contraction, apoptosis, memory, inflammation and the immune response. In this minireview, we analyze the large number of CaM-complex structures deposited in the Protein Data Bank (i.e. crystal and nuclear magnetic resonance structures) to gain insight into the structural diversity of CaM-binding sites and mechanisms, such as those for CaM-activated protein kinases and phosphatases, voltage-gated Ca(2+)-channels and the plasma membrane Ca(2+)-ATPase.
authors.affiliation: Centre for Membrane Pumps in Cells and Disease - PUMPkin, Aarhus University, Denmark; Department of Molecular Biology and Genetics, Aarhus University, Denmark.
authors.forename: Henning
authors.initials: H
authors.lastname: Tidow
authors.forename: Poul
authors.initials: P
authors.lastname: Nissen
mesh_terms: D000818:Animals; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism*; D002147:Calmodulin / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D009219:Myosin-Light-Chain Kinase / Q000378:metabolism; D011485:Protein Binding
chemical_list: D002147:Calmodulin; D009219:Myosin-Light-Chain Kinase; D002118:Calcium
keywords: EF-hands; calcium; calmodulin; calmodulin-binding site; ion channels