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

By M. Pearson, David Reczek, A. Bretscher, Paul Karplus. Cell, 2000

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Small but versatile: the extraordinary functional and structural diversity of the β-grasp fold (2007, background): “2) The doublecortin (DCX) (PDB: 1MJD [30]), RA (PDB: 1C1Y [31]), PB1 (PDB: 1IPG [32]), and FERM N-terminal domains (PDB: 1EF1 [33]), which function as adaptors in animal signaling proteins and apoptosis regulators by mediating protein-protein interactions.”
ERM proteins and merlin: integrators at the cell cortex (2002, background): “So far, three structures have been reported: a complex between the FERM domain of moesin (residues 1–297) and its C-ERMAD (residues 467–577”
Intracellular signalling controlling integrin activation in lymphocytes (2005, background): “However, the structure of moesin revealed that its FERM domain was masked by an extended actin-binding tail domai”
The role of JAK-STAT signaling pathway and its regulators in the fate of T helper cells (2017, background): “FERM domain consists of three subdomains F1, F2 &F3, which are structurally similar to Ubiquitin, CoA binding and pleckstrin homologyphosphotyrosine binding domains, respectively [21].”
Organizing the Cell Cortex: The role of ERM proteins (2010, background): “, which lies on the FERM–C-ERMAD interface directly opposite Thr567 (Ref”