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Site-directed mutagenesis was used to map the ligand-binding surface of the type II transforming growth factor-β receptor extracellular domain (TβRII-ECD). Two putative ligand-binding sites were probed, the first being a predicted hydrophobic patch, the second being the finger 1 surface loop. Nine residues were mutated in the context of full-length TβRII and the effect of these mutations on ligand-binding...
Six charged amino acid residues located in the ectodomain of the full-length type I transforming growth factor (TGF)-β receptor were individually mutated to alanine. Mutation of residues D47, D98, K102 and E104 resulted in functionally impaired receptors as demonstrated by a marked decrease in ligand-dependent signaling and ligand internalization relative to the wild-type receptor. The other two mutants...
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