Structural diversity of calmodulin binding to its target sites

• Published in: The FEBS journal Vol. 280; no. 21; pp. 5551 - 5565
• Main Authors: Tidow, Henning, Nissen, Poul
• Format: Journal Article
• Language: English
• Published: England Published by Blackwell Pub. on behalf of the Federation of European Biochemical Societies 01.11.2013; Blackwell Publishing Ltd
• Subjects: Animals; apoptosis; Binding Sites; Ca2-transporting ATPase; calcium; Calcium - metabolism; calmodulin; Calmodulin - chemistry; Calmodulin - metabolism; calmodulin‐binding site; EF‐hands; Humans; immune response; inflammation; ion channels; Kinases; memory; metabolism; Models, Molecular; muscle contraction; Myosin-Light-Chain Kinase - metabolism; nuclear magnetic resonance spectroscopy; Olea; plasma membrane; plasma membranes; Protein Binding; protein kinase; protein kinases; Proteins; calcium; calmodulin; calmodulin-binding site; EF-hands; ion channels
• ISSN: 1742-464X; 1742-4658; 1742-4658
• DOI: 10.1111/febs.12296

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 Ca²⁺‐channels and the plasma membrane Ca²⁺‐ATPase.