Skip to main content
. 2011 Mar 18;30(7):1263–1276. doi: 10.1038/emboj.2011.54

Figure 1.

Figure 1

Structure of the TGF-β receptor complex and effect of ligand monomerization. (A) Surface representation of the TGF-β3 homodimer bound to the TβRI and TβRII extracellular domains (PDB 2PJY). The two protomers of TGF-β3 are depicted in pink and dark blue. TβRII binds to the fingertips of each protomer and is depicted in green, whereas TβRI binds to the underside of the fingers and is depicted in yellow. The residues in the interface between TGF-β3 and TβRII are shown in the expanded view shown on the right. (B) Schematic representation of the TGF-β3 receptor complex where high affinity TβRI binding is dependent upon interactions with both TGF-β3 protomers and TβRII. (C) Schematic representation of the TGF-β3 monomer, which binds TβRII with the same affinity as wild-type TGF-β3, but which is impaired in its ability to bind and recruit TβRI. (D) Schematic representation of a TGF-β3 heterodimer comprising a wild-type protomer (blue) and a variant (pink) bearing substitutions that block TβRI and TβRII binding.