| Autor: |
Pepin, Marie-Claude, Beauchemin, Michel, Plamondon, Josée, O'Connor-McCourt, Maureen D. |
| Zdroj: |
Biochemical and Biophysical Research Communications; March 1996, Vol. 220 Issue: 2 p289-293, 5p |
| Abstrakt: |
There are three main types of receptors for TGF-β termed receptor type I, type II and type III. TGF-β receptor type II has a crucial role in the cell's responsiveness to TGF-β as it is mandatory for TGF-β binding to the signaling complex (receptor type I and type II). Here we have used a scanning-deletion mutagenesis approach to determine the core binding domain of the extracellular domain of receptor type II that is required for interaction with TGF-β. Deletions of three amino acids were systematically introduced at intervals of five amino acids in order to scan the N- and C-terminus of the extracellular domain of the receptor. We find that the N-terminal region which is devoid of cysteine residues is not critical for ligand binding. Similarly, the C-terminal region, i.e., the amino acids flanking the transmembrane domain, are dispensable for binding. These results suggest that the central 100 amino acid span that is rich in cysteine residues is the core binding domain for TGF-β. |
| Databáze: |
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