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PDBsum entry 1ef1
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Membrane protein
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PDB id
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1ef1
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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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Structure of the erm protein moesin reveals the ferm domain fold masked by an extended actin binding tail domain.
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Authors
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M.A.Pearson,
D.Reczek,
A.Bretscher,
P.A.Karplus.
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Ref.
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Cell, 2000,
101,
259-270.
[DOI no: ]
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PubMed id
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Abstract
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The ezrin-radixin-moesin (ERM) protein family link actin filaments of cell
surface structures to the plasma membrane, using a C-terminal F-actin binding
segment and an N-terminal FERM domain, a common membrane binding module. ERM
proteins are regulated by an intramolecular association of the FERM and
C-terminal tail domains that masks their binding sites. The crystal structure of
a dormant moesin FERM/tail complex reveals that the FERM domain has three
compact lobes including an integrated PTB/PH/ EVH1 fold, with the C-terminal
segment bound as an extended peptide masking a large surface of the FERM domain.
This extended binding mode suggests a novel mechanism for how different signals
could produce varying levels of activation. Sequence conservation suggests a
similar regulation of the tumor suppressor merlin.
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Figure 6.
Figure 6. Stereodiagram of the Region Surrounding
Thr558Thr558 is in van der Waals contact with FERM residues
Thr235 and Pro236, and is accessible to solvent from the right
between the side chains of Arg553, Lys557, and Gln561. The
electron density (from an NCS averaged map calculated with
coefficients 2F[O] − 2F[C], αC) is contoured at 2.2 ×
ρ[rms]. A phosphoryl group modeled onto Thr558 collides with
surrounding atoms from Arg553 and Gln561.
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Figure 7.
Figure 7. Potential FERM Domain Interaction SitesThe
positions of five binding sites on proteins that are
structurally similar to the three FERM lobes are indicated: (1)
by analogy with the protein interaction site seen for elongin B
([62]) and the Ras binding domain of Raf kinase ( [47]);
(2) by analogy with the lipid binding site of the acyl CoA
binding protein ( [36]), but this site is blocked by the loop
connecting the F2 helices C and D; (3) by analogy with the
proline-containing peptide binding site on EVH1 domains ( [53];
Federov et al., 1999); (4) by analogy with the canonical peptide
binding site of PTB domains ( [74]); and (5) by analogy with the
inositol phosphate binding sites on PH domains ( [13 and 31]).
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The above figures are
reprinted
by permission from Cell Press:
Cell
(2000,
101,
259-270)
copyright 2000.
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