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Structural Diversity in Calmodulin - Peptide Interactions

[ Vol. 20 , Issue. 11 ]

Author(s):

Zsolt Dürvanger* and Veronika Harmat   Pages 1102 - 1111 ( 10 )

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.

Affiliation:

Laboratory of Structural Chemistry and Biology, Institute of Chemistry, Eötvös Loránd University, Budapest, Laboratory of Structural Chemistry and Biology, Institute of Chemistry, Eötvös Loránd University, Budapest

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