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Ligand binding by fibroblast growth factor receptors investigated using chimeric receptor molecules.

作者信息

Yayon A, Gray T E, Zimmer Y, Eisenstein M, Givol D

机构信息

Department of Chemical Immunology, Weizmann Institute of Science, Rehovot, Israel.

出版信息

J Recept Signal Transduct Res. 1995 Jan-Mar;15(1-4):185-97. doi: 10.3109/10799899509045216.

DOI:10.3109/10799899509045216
PMID:8903940
Abstract

In order to map in detail the ligand binding sites of fibroblast growth factor receptor 2 (FGFR2) and keratinocyte growth factor receptor (KGFR), we have generated receptor molecules that are chimeric within the membrane proximal sequence that varies between them. The chimeric molecules are found to bind aFGF with a greater than 5-fold difference in affinity, indicating that there is coupling between the chimeric regions with respect to aFGF binding. Further, binding of bFGF and KGF is abolished in the chimeras, showing that the binding site for these ligands requires the whole of the 48- or 50- amino acid variable sequence to be intact. Direct interactions between the different regions exchanged in the chimeras are most probably involved in forming KGF or bFGF binding sites.

摘要

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