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A discrete domain of the human TrkB receptor defines the binding sites for BDNF and NT-4

Robertson, Alan G.S.; Mason, Grant G.F.; Dawbarn, David; Wilcock, Gordon K.; Clarke, Anthony R.; Burston, Judy J.; Sessions, Richard B.; Naylor, Ruth L.; Allen, Shelley J.; Tyler, Sue J.


Alan G.S. Robertson

Grant G.F. Mason

David Dawbarn

Gordon K. Wilcock

Anthony R. Clarke

Judy J. Burston

Richard B. Sessions

Ruth L. Naylor

Shelley J. Allen

Sue J. Tyler


TrkB is a member of the Trk family of tyrosine kinase receptors. In vivo, the extracellular region of TrkB is known to bind, with high affinity, the neurotrophin protein brain-derived neurotrophic factor (BDNF) and neurotrophin-4 (NT-4). We describe the expression and purification of the second Ig-like domain of human TrkB (TrkBIg2) and show, using surface plasmon resonance, that this domain is sufficient to bind BDNF and NT-4 with subnanomolar affinity. BDNF and NT-4 may have therapeutic implications for a variety of neurodegenerative diseases. The specificity of binding of the neurotrophins to their receptor TrkB is therefore of interest. We examine the specificity of TrkBIg2 for all the neurotrophins, and use our molecular model of the BDNF-TrkBIg2 complex to examine the residues involved in binding. It is hoped that the understanding of specific interactions will allow design of small molecule neurotrophin mimetics. © 2002 Elsevier Science (USA).


Wilcock, G. K., Dawbarn, D., Mason, G. G., Robertson, A. G., Clarke, A. R., Burston, J. J., …Tyler, S. J. (2002). A discrete domain of the human TrkB receptor defines the binding sites for BDNF and NT-4. Biochemical and Biophysical Research Communications, 291(3), 501-507.

Journal Article Type Article
Publication Date Jan 1, 2002
Journal Biochemical and Biophysical Research Communications
Print ISSN 0006-291X
Publisher Elsevier
Peer Reviewed Not Peer Reviewed
Volume 291
Issue 3
Pages 501-507
Keywords brain-derived neurotrophic factor, molecular model, neurotrophin-4, receptor protein-tyrosine kinases, receptor, TrkB, surface plasmon resonance
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