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Structure of dimerized radixin FERM domain suggests a novel masking motif in C-terminal residues 295-304.

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.

SUBMITTER: Kitano K

PROVIDER: S-EPMC2222584 | biostudies-literature | 2006 Apr

REPOSITORIES: biostudies-literature

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Structure of dimerized radixin FERM domain suggests a novel masking motif in C-terminal residues 295-304.

Kitano Ken K Yusa Fumie F Hakoshima Toshio T

Acta crystallographica. Section F, Structural biology and crystallization communications 20060325 Pt 4

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 si ...[more]

PMID: 16582480

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