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PDBsum entry 1e5w
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Membrane protein
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PDB id
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1e5w
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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The 2.7 a crystal structure of the activated ferm domain of moesin: an analysis of structural changes on activation.
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Authors
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S.D.Edwards,
N.H.Keep.
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Ref.
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Biochemistry, 2001,
40,
7061-7068.
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PubMed id
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Abstract
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Moesin binds to a large range of proteins through its N terminal FERM (band 4.1,
ezrin, radixin, moesin) domain. In full-length moesin isolated from cells, this
binding is masked by binding to the C-terminal domain of moesin (C-ERMAD).
Activation takes place by phosphorylation of Thr 558 in the C-ERMAD, which
releases the C-ERMAD. A recently determined crystal structure of a noncovalent
complex of the FERM and C-ERMAD domains showed for the first time that the
structure of the FERM domain consists of three subdomains, each of which is
similar to known structures. The structure reported here also contains a unique
47-residue helix pointing away from the FERM domain at the start of the alpha
domain, in agreement with secondary structure predictions. Removal of the
C-ERMAD does not result in a huge rearrangement of the FERM domain, but
comparison with the activated radixin structure shows a consistent set of small
changes. Not surprisingly, the exposed C-ERMAD binding area interacts in crystal
contacts. More interestingly, a negatively charged peptide binds to the inositol
site in a crystal contact and causes a greater conformational change in the
structure than inositol.
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