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PDBsum entry 4rm9
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Peptide binding protein
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PDB id
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4rm9
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References listed in PDB file
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Key reference
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Title
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Structural characterization suggests models for monomeric and dimeric forms of full-Length ezrin.
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Authors
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J.M.Phang,
S.J.Harrop,
A.P.Duff,
A.V.Sokolova,
B.Crossett,
J.C.Walsh,
S.A.Beckham,
C.D.Nguyen,
R.B.Davies,
C.Glöckner,
E.H.Bromley,
K.E.Wilk,
P.M.Curmi.
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Ref.
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Biochem J, 2016,
473,
2763-2782.
[DOI no: ]
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PubMed id
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Abstract
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Ezrin is a member of the ERM (ezrin-radixin-moesin) family of proteins that have
been conserved through metazoan evolution. These proteins have dormant and
active forms, where the latter links the actin cytoskeleton to membranes. ERM
proteins have three domains: an N-terminal FERM [band Four-point-one (4.1) ERM]
domain comprising three subdomains (F1, F2, and F3); a helical domain; and a
C-terminal actin-binding domain. In the dormant form, FERM and C-terminal
domains form a stable complex. We have determined crystal structures of the
active FERM domain and the dormant FERM:C-terminal domain complex of human
ezrin. We observe a bistable array of phenylalanine residues in the core of
subdomain F3 that is mobile in the active form and locked in the dormant form.
As subdomain F3 is pivotal in binding membrane proteins and phospholipids, these
transitions may facilitate activation and signaling. Full-length ezrin forms
stable monomers and dimers. We used small-angle X-ray scattering to determine
the solution structures of these species. As expected, the monomer shows a
globular domain with a protruding helical coiled coil. The dimer shows an
elongated dumbbell structure that is twice as long as the monomer. By aligning
ERM sequences spanning metazoan evolution, we show that the central helical
region is conserved, preserving the heptad repeat. Using this, we have built a
dimer model where each monomer forms half of an elongated antiparallel coiled
coil with domain-swapped FERM:C-terminal domain complexes at each end. The model
suggests that ERM dimers may bind to actin in a parallel fashion.
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