TGFβ receptors are single pass serine/threonine kinase receptors. They exist in several different isoforms that can be homo- or heterodimeric.[1] The number of characterized ligands in the TGFβ superfamily far exceeds the number of known receptors, suggesting the promiscuity that exists between the ligand and receptor interactions.
Three TGF-β receptor types can be distinguished by their structural and functional properties. Receptor types I and II have similar ligand-binding affinities and can be distinguished from each other only by peptide mapping. Both receptor types I and II have a high affinity for TGF-β1 and low affinity for TGF-β2. TGF-β receptor type III has a high affinity for both TGF-β1 and -β2 and in addition TGF-β1.2.[2]
^Doré Jr, J. J.; Edens, M.; Garamszegi, N.; Leof, E. B. (1998). "Heteromeric and homomeric transforming growth factor-beta receptors show distinct signaling and endocytic responses in epithelial cells". The Journal of biological chemistry. 273 (48): 31770–31777. doi:10.1074/jbc.273.48.31770. PMID9822641.{{cite journal}}: CS1 maint: unflagged free DOI (link) (free full text)
^Cheifetz, S.; Andres, J. L.; Massagué, J. (1988). "The transforming growth factor-beta receptor type III is a membrane proteoglycan. Domain structure of the receptor". The Journal of biological chemistry. 263 (32): 16984–16991. PMID2903157.
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