Structural Diversity in Calmodulin - Peptide Interactions

Author(s): Zsolt Dürvanger*, Veronika Harmat.

Journal Name: Current Protein & Peptide Science

Volume 20 , Issue 11 , 2019

Become EABM
Become Reviewer

Graphical Abstract:


Abstract:

Calmodulin (CaM) is a highly conserved eukaryotic Ca2+ sensor protein that is able to bind a large variety of target sequences without a defined consensus sequence. The recognition of this diverse target set allows CaM to take part in the regulation of several vital cell functions. To fully understand the structural basis of the regulation functions of CaM, the investigation of complexes of CaM and its targets is essential. In this minireview we give an outline of the different types of CaM - peptide complexes with 3D structure determined, also providing an overview of recently determined structures. We discuss factors defining the orientations of peptides within the complexes, as well as roles of anchoring residues. The emphasis is on complexes where multiple binding modes were found.

Keywords: Calcium, calmodulin, EF-hands, calmodulin-peptide complexes, protein-peptide interaction, binding motifs.

Rights & PermissionsPrintExport Cite as

Article Details

VOLUME: 20
ISSUE: 11
Year: 2019
Page: [1102 - 1111]
Pages: 10
DOI: 10.2174/1389203720666190925101937
Price: $58

Article Metrics

PDF: 11