FERM domain

FERM N-terminal domain
crystal structure of the ferm domain of merlin, the neurofibromatosis 2 tumor suppressor protein.
Identifiers
SymbolFERM_N
PfamPF09379
Pfam clanCL0072
InterProIPR018979
SCOP21gc7 / SCOPe / SUPFAM
OPM superfamily49
OPM protein1gc6
Membranome161
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
FERM central domain
crystal structure of the protein 4.1r membrane binding domain
Identifiers
SymbolFERM_M
PfamPF00373
InterProIPR019748
SCOP21gc7 / SCOPe / SUPFAM
CDDcd14473
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
FERM C-terminal PH-like domain
crystal structure of the radixin ferm domain complexed with the nep cytoplasmic tail
Identifiers
SymbolFERM_C
PfamPF09380
Pfam clanCL0266
InterProIPR018980
SCOP21ef1 / SCOPe / SUPFAM
CDDcd00836
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

In molecular biology, the FERM domain (F for 4.1 protein, E for ezrin, R for radixin and M for moesin) is a widespread protein module involved in localising proteins to the plasma membrane.[1] FERM domains are found in a number of cytoskeletal-associated proteins that associate with various proteins at the interface between the plasma membrane and the cytoskeleton. The FERM domain is located at the N terminus in the majority of proteins in which it is found.[1][2]

  1. ^ a b Chishti AH, Kim AC, Marfatia SM, Lutchman M, Hanspal M, Jindal H, Liu SC, Low PS, Rouleau GA, Mohandas N, Chasis JA, Conboy JG, Gascard P, Takakuwa Y, Huang SC, Benz EJ, Bretscher A, Fehon RG, Gusella JF, Ramesh V, Solomon F, Marchesi VT, Tsukita S, Tsukita S, Hoover KB (August 1998). "The FERM domain: a unique module involved in the linkage of cytoplasmic proteins to the membrane". Trends Biochem. Sci. 23 (8): 281–2. doi:10.1016/S0968-0004(98)01237-7. PMID 9757824.
  2. ^ Pearson MA, Reczek D, Bretscher A, Karplus PA (April 2000). "Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain". Cell. 101 (3): 259–70. doi:10.1016/S0092-8674(00)80836-3. PMID 10847681. S2CID 7119092.