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

Item Type:Review
Title:Ligand-binding sites in Ig-like domains of receptor tyrosine kinases
Creators Name:Wiesmann, C. and Muller, Y.A. and de Vos, A.M.
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.
Keywords:Binding and Specificity, Crystal Structure, Flt-1, Ig-like Domain, Ligand- Receptor Complex, TrkA
Source:Journal of Molecular Medicine
ISSN:0946-2716
Publisher:Springer (Germany)
Volume:78
Number:5
Page Range:247-260
Date:1 January 2000
Official Publication:https://doi.org/10.1007/s001090000082
PubMed:View item in PubMed

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