Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain.

The ezrin-radixin-moesin (ERM) protein family link actin filaments of cell surface structures to the plasma membrane, using a C-terminal F-actin binding segment and an N-terminal FERM domain, a common membrane binding module. ERM proteins are regulated by an intramolecular association of the FERM and C-terminal tail domains that masks their ...
binding sites. The crystal structure of a dormant moesin FERM/tail complex reveals that the FERM domain has three compact lobes including an integrated PTB/PH/ EVH1 fold, with the C-terminal segment bound as an extended peptide masking a large surface of the FERM domain. This extended binding mode suggests a novel mechanism for how different signals could produce varying levels of activation. Sequence conservation suggests a similar regulation of the tumor suppressor merlin.
Mesh Terms:
Actins, Amino Acid Sequence, Binding Sites, Crystallography, X-Ray, Cytoskeletal Proteins, Humans, Membrane Proteins, Microfilament Proteins, Models, Molecular, Molecular Sequence Data, Neurofibromin 2, Neuropeptides, Protein Folding, Protein Structure, Tertiary, Recombinant Fusion Proteins
Cell
Date: Apr. 28, 2000
Download Curated Data For This Publication
8814
Switch View:
  • Interactions 1