Abstract
Calmodulin (CaM) is a prototypical Ca2+-sensor protein that can control many important biological functions by binding to hundreds of target proteins. To gain insight into the versatility of CaM-target recognition, we have analyzed the complex structures for many types of CaM-binding peptides and some target proteins. In particular, some recently reported novel complex structures reveal that the versatile target binding of CaM is accommodated by its flexible domain arrangement and the malleability of its interfaces.
MeSH Terms
Animals
Calcium/metabolism
Calcium-Calmodulin-Dependent Protein Kinase Kinase
Calcium-Transporting ATPases/metabolism
Calmodulin/chemistry,metabolism
Calmodulin-Binding Proteins/metabolism
Cell Membrane/metabolism
Cytoskeletal Proteins/metabolism
Glutamate Decarboxylase/metabolism
Intracellular Signaling Peptides and Proteins/metabolism
Membrane Proteins/metabolism
Models, Molecular
Myristoylated Alanine-Rich C Kinase Substrate
Nerve Tissue Proteins/metabolism
Nitric Oxide Synthase Type III/metabolism
Peptides/genetics,metabolism
Plant Proteins/metabolism
Protein Binding
Protein Conformation
Protein Serine-Threonine Kinases/metabolism
Sequence Analysis, Protein
Small-Conductance Calcium-Activated Potassium Channels/metabolism
Viper Venoms/metabolism
Chemicals
Basp1 protein, mouse
Calmodulin
Calmodulin-Binding Proteins
Cytoskeletal Proteins
Intracellular Signaling Peptides and Proteins
Membrane Proteins
Nerve Tissue Proteins
Peptides
Plant Proteins
Small-Conductance Calcium-Activated Potassium Channels
Viper Venoms
edema factor
Myristoylated Alanine-Rich C Kinase Substrate
Nitric Oxide Synthase Type III
Protein Serine-Threonine Kinases
Calcium-Calmodulin-Dependent Protein Kinase Kinase
Glutamate Decarboxylase
Calcium-Transporting ATPases
Calcium
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Ishida Hiroaki
Structural Biology Research Group, Department of Biological Sciences, University of Calgary, Calgary, Alberta, T2N 1N4, Canada.
Vogel Hans J