Immunoglobulin-like domains define the nerve growth factor binding site of the TrkA receptor.

Journal article

Nerve growth factor (NGF) is involved in the development and maintenance of the nervous system. NGF binds with high affinity to the extracellular region of the tyrosine kinase receptor TrkA. This domain comprises leucine and cysteine rich motifs, followed by two immunoglobulin like (Ig-like) domains. We describe the expression and purification of recombinant Ig-like domains. Fluorescence and circular dichroism spectroscopy show that the protein is folded into a compact globular structure and contains mainly beta-sheet secondary structure. Recombinant protein binds to NGF and can inhibit NGF bioactivity both in vitro and in vivo.

Authors: Holden, P; Asopa, V; Robertson, A; Clarke, A; Tyler, S

• Publication status: Published
• Journal: Nature biotechnology
• Volume: 15
• Issue: 7
• Pages: 668-672
• Publication date: 1997-07-01
• DOI: 10.1038/nbt0797-668
• EISSN: 1546-1696
• ISSN: 1087-0156
• Language: English
• Keywords: Amino Acid Sequence; Rats, Wistar; Proto-Oncogene Proteins; Protein Structure, Secondary; Binding Sites; Molecular Sequence Data; Spectrometry, Fluorescence; Protein Folding; Animals; Male; Receptor Protein-Tyrosine Kinases; Biotechnology; Binding, Competitive; Nerve Growth Factors; Circular Dichroism; Humans; PC12 Cells; Rats; Recombinant Proteins; Receptor, trkA; Receptors, Nerve Growth Factor; Immunoglobulins