Structural Diversity in Calmodulin - Peptide Interactions.

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.

journal_name

Curr Protein Pept Sci

authors

Dürvanger Z,Harmat V

doi

10.2174/1389203720666190925101937

subject

Has Abstract

pub_date

2019-01-01 00:00:00

pages

1102-1111

issue

11

eissn

1389-2037

issn

1875-5550

pii

CPPS-EPUB-100987

journal_volume

20

pub_type

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