1EF1

CRYSTAL STRUCTURE OF THE MOESIN FERM DOMAIN/TAIL DOMAIN COMPLEX

Summary for 1EF1

• Entry DOI: 10.2210/pdb1ef1/pdb
• Descriptor: MOESIN, SULFATE ION, ... (4 entities in total)
• Functional Keywords: membrane, ferm domain, tail domain, membrane protein
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 4
• Total formula weight: 91023.36

Authors

Pearson, M.A.,Reczek, D.,Bretscher, A.,Karplus, P.A. (deposition date: 2000-02-04, release date: 2000-05-10, Last modification date: 2024-11-06)

Primary citation

Pearson, M.A.,Reczek, D.,Bretscher, A.,Karplus, P.A.
Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain.
Cell(Cambridge,Mass.), 101:259-270, 2000

PubMed Abstract: 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.

PubMed: 10847681
DOI: 10.1016/S0092-8674(00)80836-3

Experimental method

X-RAY DIFFRACTION (1.9 Å)