Structure-Function Analysis of Hepatocyte Growth Factor and its Tyrosine-Kinase Receptor c-Met
| Autor: | Paul J. Godowski, Nathalie A. Lokker, Melanie R. Mark |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
biology
Fibroblast growth factor receptor 2 Chemistry Fibroblast growth factor receptor 4 Fibroblast growth factor receptor 3 Receptor tyrosine kinase Cell biology Growth factor receptor Hepatocyte Growth Factor Receptor biology.protein medicine Hepatocyte growth factor Hepatocyte nuclear factor 4 gamma medicine.drug |
| Zdroj: | Tyrosine Phosphorylation/Dephosphorylation and Downstream Signalling ISBN: 9783642782497 |
| Popis: | Hepatocyte growth factor (HGF) exhibits mitogenic and/or motogenic activities for a variety of cells (see for review Matsumoto and Nakamura, 1992). Structurally, it has similarities to kringle-containing serine-proteases, although it does not possess proteolytic activity. The HGF receptor (HGFr) is the product of the c-met proto-oncogene, a membrane-spanning tyrosine kinase receptor. The 190-kDa precursor is proteolytically processed within the extra-cellular domain (ECD) to a heterodimer consisting of a 50-kDa α subunit disufide-linked to a 145-kDa β subunit. A structure-activity relationship analysis of both HGF and its receptor was performed by functional analysis of ligand and receptor variants. |
| Databáze: | OpenAIRE |
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