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Structural basis for the activation of FGFR by NCAM

¹ University of Copenhagen;
² Hagedorn Research Institute

(RECEIVED April 24, 2008; ACCEPTED June 24, 2008)

The fibroblast growth factor receptor (FGFR) can be activated through direct interaction with the neural cell adhesion molecule (NCAM). The extracellular part of FGFR consists of three immunoglobulin-like (Ig) modules, and that of NCAM consists of five Ig and two fibronectin type III (F3) modules. NCAM-FGFR interactions are mediated by the third FGFR Ig module and the second NCAM F3 module. Using surface plasmon resonance and nuclear magnetic resonance analyses, the present study demonstrates that the second Ig module of FGFR also is involved in binding to NCAM. The second Ig module residues involved in binding were identified and shown to be localized on the "opposite sides" of the module, indicating that when NCAM molecules are clustered (e.g. due to homophilic binding), high affinity FGFR binding sites may be formed by the neighbouring NCAM molecules.

Keywords: Structure; F3 module; FGF receptor; NCAM; NMR spectroscopy; surface plasmon resonance spectroscopy

³ E-mail: arthur{at}sund.ku.dk

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