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

Journal article

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 (TrkBIg(2)) 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 i...

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Authors: Naylor, R; Robertson, A; Allen, S; Sessions, R; Clarke, A

• Publication status: Published
• Journal: Biochemical and biophysical research communications
• Volume: 291
• Issue: 3
• Pages: 501-507
• Publication date: 2002-03-01
• DOI: 10.1006/bbrc.2002.6468
• EISSN: 1090-2104
• ISSN: 0006-291X
• Language: English
• Keywords: Receptor, trkB; Humans; Models, Molecular; Molecular Sequence Data; Nerve Growth Factors; Binding Sites; Kinetics; Immunoglobulin Fragments; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Sequence Homology, Amino Acid; Protein Structure, Tertiary; Surface Plasmon Resonance; Amino Acid Sequence; Circular Dichroism; Brain-Derived Neurotrophic Factor