Abstract.
Receptor tyrosine kinases are cell-bound, membrane-spanning receptors that transduce growth factor dependent signals to the intracellular environment. Their catalytic cytoplasmic domains share a high level of sequence similarity, but their extracellular portions usually have a highly variable, multiple-domain structure. In a growing number of cases immunoglobulin-like domains contained within the extracellular portion have been shown to contain the ligand-binding site. In recent years experimental three-dimensional structures have been determined for some of these domains, free or in complex with their ligand. Here we review current structural information on these immunoglobulin-like domains and the growth factors that bind to them, with an emphasis on the vascular endothelial growth factor, nerve growth factor, and fibroblast growth factor systems.
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Wiesmann, C., Muller, Y. & de Vos, A. Ligand-binding sites in Ig-like domains of receptor tyrosine kinases. J Mol Med 78, 247–260 (2000). https://doi.org/10.1007/s001090000082
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DOI: https://doi.org/10.1007/s001090000082