ArticleActa crystallographica. Section F, Structural biology and crystallization communications2006
Structure of dimerized radixin FERM domain suggests a novel masking motif in C-terminal residues 295-304.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Major clinical improvement in a boy with developmental disabilities and a PTPN4 mutation with intensive re-education and an enriched environment in a day care hospital: a case report.Journal of medical case reports · 2026Article
- A somatic mutation in moesin drives progression into acute myeloid leukemia.Science advances · 2022Article
- Targeting GABAFrontiers in molecular neuroscience · 2019Article
- Binding of moesin and ezrin to membranes containing phosphatidylinositol (4,5) bisphosphate: a comparative study of the affinity constants and conformational changes.Biochimica et biophysica acta · 2012Article
- Unfurling of the band 4.1, ezrin, radixin, moesin (FERM) domain of the merlin tumor suppressor.Protein science : a publication of the Protein Society · 2011Article
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3 authors.
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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.
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