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PDBsum entry 1cvs
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Growth factor/growth factor receptor
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PDB id
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1cvs
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Contents |
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129 a.a.
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211 a.a.
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196 a.a.
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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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Structural basis for fgf receptor dimerization and activation.
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Authors
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A.N.Plotnikov,
J.Schlessinger,
S.R.Hubbard,
M.Mohammadi.
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Ref.
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Cell, 1999,
98,
641-650.
[DOI no: ]
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PubMed id
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Abstract
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The crystal structure of FGF2 bound to a naturally occurring variant of FGF
receptor 1 (FGFR1) consisting of immunoglobulin-like domains 2 (D2) and 3 (D3)
has been determined at 2.8 A resolution. Two FGF2:FGFR1 complexes form a 2-fold
symmetric dimer. Within each complex, FGF2 interacts extensively with D2 and D3
as well as with the linker between the two domains. The dimer is stabilized by
interactions between FGF2 and D2 of the adjoining complex and by a direct
interaction between D2 of each receptor. A positively charged canyon formed by a
cluster of exposed basic residues likely represents the heparin-binding site. A
general model for FGF- and heparin-induced FGFR dimerization is inferred from
the crystal structure, unifying a wealth of biochemical data.
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Figure 4.
Figure 4. Mapping of the Different Interaction Sites onto
the Molecular Surfaces of FGF2 and FGFR1The surface color
codings for D2, D3, the linker, and FGF2 are the same as in
Figure 1. The surfaces of FGF2 and FGFR1 that form the primary
and secondary interaction sites are shown in red and purple,
respectively. The heparin-binding surfaces are depicted in blue.
The surface on D2 engaged in direct receptor–receptor
interaction is colored yellow. To better visualize the different
functional surfaces on FGF2 and D23, the two molecules are
pulled away from each other and rotated 90° about the
vertical axis. This figure was created using the program GRASP (
[33]).
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Figure 5.
Figure 5. The Primary Interaction Site between FGF2 and
FGFR1(A) Stereo view of the hydrophobic interface between FGF2
and D2 of FGFR1. Only side chains of interacting residues are
shown. Color coding is the same as in Figure 1: FGF2 in orange,
D2 in green, D3 in blue, and the linker in gray. Dotted lines
represent hydrogen bonds.(B) Stereo view of the network of
hydrogen bonds between FGF2 and FGFR1 in the vicinity of Arg-250
in the D2–D3 linker.(C) Stereo view of the interface between
FGF2 and D3 of FGFR1. This figure was created using the programs
Molscript and Raster3D.
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The above figures are
reprinted
by permission from Cell Press:
Cell
(1999,
98,
641-650)
copyright 1999.
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