NGF binding to the trk tyrosine kinase receptor requires the extracellular immunoglobulin-like domains. Academic Article uri icon

Overview

abstract

  • Neurotrophins initiate their biological effects by activating members of the trk tyrosine kinase subfamily. The extracellular region of trk receptors is distinguished by several common structural features, including leucine-rich repeats, clusters of cysteine-rich domains, and two immunoglobulin-like domains. However, the receptor sequences required for ligand binding have not been localized. In order to define the domains involved in NGF binding, a series of chimeric receptors was constructed using cDNA sequences from rat trkA and trkB. The chimeric constructs were expressed after transient transfection in 293 cells and the expression of each receptor was verified by immunoprecipitation and immunoblot analysis. Equilibrium binding of transfected cells revealed that the two IgG domains of trkA are essential for NGF binding. The requirement for the two IgG domains was further confirmed by Scatchard analysis and affinity crosslinking with 125I-NGF. These results indicate that NGF binding is crucially dependent upon interactions with the IgG domains of the trkA receptor.

publication date

  • April 1, 1995

Research

keywords

  • Nerve Growth Factors
  • Receptor Protein-Tyrosine Kinases

Identity

Scopus Document Identifier

  • 0029017053

PubMed ID

  • 7551570

Additional Document Info

volume

  • 6

issue

  • 2