BAIT
MSN
HEL70
moesin
GO Process (7)
GO Function (6)
GO Component (12)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
MSN
HEL70
moesin
GO Process (7)
GO Function (6)
GO Component (12)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
Co-crystal Structure
Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.
Publication
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 ... [more]
Cell Apr. 28, 2000; 101(3);259-70 [Pubmed: 10847681]
Throughput
- Low Throughput
Additional Notes
- domain-domain contacts
Curated By
- BioGRID