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PDBsum entry 2bkd
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Nuclear protein
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PDB id
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2bkd
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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 structure of the n-Terminal domain of the fragile X mental retardation protein: a platform for protein-Protein interaction.
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Authors
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A.Ramos,
D.Hollingworth,
S.Adinolfi,
M.Castets,
G.Kelly,
T.A.Frenkiel,
B.Bardoni,
A.Pastore.
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Ref.
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Structure, 2006,
14,
21-31.
[DOI no: ]
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PubMed id
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Abstract
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FMRP, whose lack of expression causes the X-linked fragile X syndrome, is a
modular RNA binding protein thought to be involved in posttranslational
regulation. We have solved the structure in solution of the N-terminal domain of
FMRP (NDF), a functionally important region involved in multiple interactions.
The structure consists of a composite fold comprising two repeats of a Tudor
motif followed by a short alpha helix. The interactions between the three
structural elements are essential for the stability of the NDF fold. Although
structurally similar, the two repeats have different dynamic and functional
properties. The second, more flexible repeat is responsible for interacting both
with methylated lysine and with 82-FIP, one of the FMRP nuclear partners. NDF
contains a 3D nucleolar localization signal, since destabilization of its fold
leads to altered nucleolar localization of FMRP. We suggest that the NDF
composite fold determines an allosteric mechanism that regulates the FMRP
functions.
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Figure 6.
Figure 6. Mapping the Interaction Surface of 82-FIP onto
the NDF Structure
(A) Exposed hydrophobic patches (green)
are shown on two surface representations of the NDF structure
(white) that differ by a 180° rotation around the y axis. The
orientation of the NDF structure on the left is the same as that
in the right panel of Figure 2B.
(B) Residues involved in
the interaction with 82-FIP156. The side chains of the residues
that lead to marked (10, 13, 32, 64, 66, 67, 68, 70, 72-75, 79,
81-89, 91-95, 98, 101, 105, 107-110, 113) and minor (9, 14-16,
33, 69, 71, 80, 102) variations of the peak intensities in the
HSQC are displayed in dark blue and light blue, respectively.
(C) Same as in (B), but in a ribbon representation showing
explicitly the side chains of the residues affected.
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2006,
14,
21-31)
copyright 2006.
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