Structures of calmodulin-melittin complexes show multiple binding modes lacking classical anchoring interactions.

ABSTRACT: Calmodulin (CaM) is a Ca²⁺ sensor protein found in all eukaryotic cells that regulates a large number of target proteins in a Ca²⁺ concentration-dependent manner. As a transient-type hub protein, it recognizes linear motifs of its targets, though for the Ca²⁺-dependent binding, no consensus sequence was identified. Its complex with melittin, a major component of bee venom, is often used as a model system of protein-protein complexes. Yet, the structural aspects of the binding are not well understood, as only diverse, low-resolution data are available concerning the association. We present the crystal structure of melittin in complex with Ca²⁺-saturated CaMs from two, evolutionarily distant species, Homo sapiens and Plasmodium falciparum, represen

SUBMITTER: Durvanger Z 

PROVIDER: S-EPMC10140167 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature