PMID:16582480

Citation	Kitano, K, Yusa, F and Hakoshima, T (2006) Structure of dimerized radixin FERM domain suggests a novel masking motif in C-terminal residues 295-304. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62:340-5
Abstract	ERM (ezrin/radixin/moesin) proteins bind to the cytoplasmic tail of adhesion molecules in the formation of the membrane-associated cytoskeleton. The binding site is located in the FERM (4.1 and ERM) domain, a domain that is masked in the inactive form. A conventional masking motif, strand 1 (residues 494-500 in radixin), has previously been identified in the C-terminal tail domain. Here, the crystal structure of dimerized radixin FERM domains (residues 1-310) is presented in which the binding site of one molecule is occupied by the C-terminal residues (residues 295-304, strand 2) of the other molecule. The residues contain a conserved motif that is compatible with that identified in the adhesion molecules. The residues might serve as a second masking region in the inactive form of ERM proteins.
Links	PubMed PMC2222584 Online version:10.1107/S1744309106010062
Keywords	Actins/metabolism; Animals; Binding Sites; Crystallography, X-Ray; Cytoskeletal Proteins/chemistry; Cytoskeletal Proteins/isolation & purification; Cytoskeletal Proteins/metabolism; Humans; Membrane Proteins/chemistry; Membrane Proteins/isolation & purification; Membrane Proteins/metabolism; Mice; Models, Molecular; Peptide Fragments/chemistry; Protein Structure, Secondary
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Significance

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
HUMAN:F5H1A7	enables	GO:0042803: protein homodimerization activity	ECO:0000250: sequence similarity evidence used in manual assertion	UniProtKB:P26043	F		Seeded From UniProt	complete

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