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PDBsum entry 1lwr
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Cell adhesion
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PDB id
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1lwr
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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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Structural basis for a direct interaction between fgfr1 and ncam and evidence for a regulatory role of ATP.
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Authors
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V.V.Kiselyov,
G.Skladchikova,
A.M.Hinsby,
P.H.Jensen,
N.Kulahin,
V.Soroka,
N.Pedersen,
V.Tsetlin,
F.M.Poulsen,
V.Berezin,
E.Bock.
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Ref.
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Structure, 2003,
11,
691-701.
[DOI no: ]
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PubMed id
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Abstract
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The neural cell adhesion molecule (NCAM) promotes axonal outgrowth, presumably
through an interaction with the fibroblast growth factor receptor (FGFR). NCAM
also has a little-understood ATPase activity. We here demonstrate for the first
modules 1 and
2) and FGFR1 (Ig modules 2 and 3) by surface plasmon resonance (SPR) analysis.
The structure of the NCAM F3 module 2 was determined by NMR and the module was
shown by NMR to interact with the FGFR1 Ig module 3 and ATP. The NCAM sites
binding to FGFR and ATP were found to overlap and ATP was shown by SPR to
inhibit the NCAM-FGFR binding, indicating that ATP probably regulates the
NCAM-FGFR interaction. Furthermore, we demonstrate that the NCAM module was able
to induce activation (phosphorylation) of FGFR and to stimulate neurite
outgrowth. In contrast, ATP inhibited neurite outgrowth induced by the module.
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Figure 2.
Figure 2. Structure of the NCAM F3 Module 2(A) Stereo view
of an overlay of the backbone atoms of 30 superimposed
structures.(B) Ribbon representation of the structure.
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2003,
11,
691-701)
copyright 2003.
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