Transforming growth factor beta (TGFβ) receptors are
single passserine/threonine kinase receptors that belong to
TGFβ receptor family. 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 TGFβ superfamily receptors specific for TGFβ, the TGFβ receptors, can be distinguished by their structural and functional properties.
TGFβR1 (ALK5) and
TGFβR2 have similar ligand-binding affinities and can be distinguished from each other only by
peptide mapping. Both TGFβR1 and TGFβR2 have a high affinity for
TGFβ1 and low affinity for
TGFβ2.
TGFβR3 (β-glycan) has a high affinity for both
homodimeric TGFβ1 and TGFβ2 and in addition the
heterodimer TGF-β1.2.[2] The TGFβ receptors also bind
TGFβ3.
Transforming growth factor beta (TGFβ) receptors are
single passserine/threonine kinase receptors that belong to
TGFβ receptor family. 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 TGFβ superfamily receptors specific for TGFβ, the TGFβ receptors, can be distinguished by their structural and functional properties.
TGFβR1 (ALK5) and
TGFβR2 have similar ligand-binding affinities and can be distinguished from each other only by
peptide mapping. Both TGFβR1 and TGFβR2 have a high affinity for
TGFβ1 and low affinity for
TGFβ2.
TGFβR3 (β-glycan) has a high affinity for both
homodimeric TGFβ1 and TGFβ2 and in addition the
heterodimer TGF-β1.2.[2] The TGFβ receptors also bind
TGFβ3.