Ligand-binding sites in Ig-like domains of receptor tyrosine kinases.

C Wiesmann, Y A Muller, A M de Vos

Journal: Journal of molecular medicine (Berlin, Germany) 2000;78(5):247-60

PMID: 10954197

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.

Address: Genentech, Inc., Department of Protein Engineering, South San Francisco, CA 94080, USA.

DOI: 10.1007/s001090000082