Abstract:
:Six charged amino acid residues located in the ectodomain of the full-length type I transforming growth factor (TGF)-beta 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 (K39A and K87A) exhibited wild-type-like activity. Molecular modeling indicates that the four functionally important residues are located on the convex face of the ectodomain structure. Since mutation of these four residues affects signaling and ligand internalization but not ligand binding, we propose that this functional site is an interacting site between type I and II receptors.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Guimond A,Sulea T,Zwaagstra JC,Ekiel I,O'Connor-McCourt MDdoi
10.1016/s0014-5793(01)03231-8keywords:
subject
Has Abstractpub_date
2002-02-27 00:00:00pages
147-52issue
2-3eissn
0014-5793issn
1873-3468pii
S0014579301032318journal_volume
513pub_type
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