TGF-beta receptor

Function TGF-β receptors (Transforming Growth Factor) (TGFBR) are serine/threonine kinase receptors. They are involved in paracrine signaling and are found in many types of tissue. TGF-β ligands include bone morphogenetic proteins, growth and initiation factors, anti-Mullerian hormone, activin, nodal TGF-β. There are 3 types of TGFBR: TGFBR I forms heteromeric complex with TGFBR II when it is bound to TGF-β. The complex transduces the TGF-β signal from the cell surface to the cytoplasm by phosphorylating proteins which regulate the transcription of genes related to cell proliferation. TGFBR I has high affinity for TGF-β1 and low affinity for TGF-β2. TGFBR II is a tumor suppressor transmembrane protein. TGFBR II has high affinity for TGF-β1 and low affinity for TGF-β2. TGFBR III is a cell-surface chondroitin sulfate / heparin sulfate proteoglycan. It acts as a reservoir of ligand for TGFBRs. TGFBR III has high affinity for TGF-β1, TGF-β2 and TGF-β1.2. Disease Over-expression of TGF causes kidney disease, diabetes and renal disease. Mutations in TGFBR II cause various types of tumors. Structural highlights TGFBR structure contains a 100-140 residues ligand-binding N-terminal extracellular domain; a transmembrane domain; a 350-400 amino acid cytoplasmic kinase domain; and a C-terminal zona pellucida (ZP) domain of ca 260 residues which has a role in protein polymerization. 3D Structures of TGF-β receptor TGF-β receptor 3D structures

spinqualitylabelsall models Human hTGFBR-II extracellular domain (green) complex with TGF-β3 (grey) (PDB code 1ktz) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

3D Structures of TGF-β receptor3D Structures of TGF-β receptor

Updated on 16-February-2020

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• TGF-β receptor I; Domains: extracellular 33-112; kinase 200-503
  • 1ias, 5e8s – hTGFBR-I kinase domain – human
    
  • 5e8t, 5e8u – hTGFBR-I kinase domain (mutant)
    
  • 5e8w, 5e8x – hTGFBR-I kinase domain (mutant) + staurosporine
    
  • 2l5s – hTGFBR-I extracellular domain - NMR
    
  • 1b6c – hTGFBR-I kinase domain + FKBP12
    
  • 1py5, 3faa, 3gxl, 3hmm, 2wot, 2wou, 3kcf, 2x7o, 3tzm, 4x0m, 4x2j, 4x2k, 4x2n, 5qim, 5fri, 4x2g, 4x2f – hTGFBR-I kinase domain + inhibitor
    
  • 5e8z, 5qik, 5qil, 5qtz, 5qu0, 6b8y, 5e90 – hTGFBR-I kinase domain (mutant) + inhibitor
    
  • 1vjy – hTGFBR-I residues 1-303 + inhibitor
    
  • 5usq – hTGFBR-I residues 123-421 + inhibitor
    
  • 1rw8 – hTGFBR-I truncated kinase domain + inhibitor
    
  • 6mac – hTGFBR-I extracellular domain + GDF-11 + activin receptor 2B-
    
• TGF-β receptor II
  • 1m9z – hTGFBR-II extracellular domain
    
  • 1plo, 4p7u – hTGFBR-II extracellular domain (mutant) - NMR
    
  • 4xjj – hTGFBR-II extracellular domain (mutant) + inhibitor
    
  • 5e8v – hTGFBR-II kinase domain (mutant)
    
  • 5e8y – hTGFBR-II kinase domain (mutant) + staurosporine
    
  • 5e92 – hTGFBR-II kinase domain (mutant) + AMPPNP
    
  • 5qin, 5e91 – hTGFBR-II kinase domain + inhibitor
    
  • 1ktz – hTGFBR-II extracellular domain + TGF-β3
    
  • 5ty4 – hTGFBR-II extracellular domain + mmTGF-β2
    
  • 5tx4 – mTGFBR-II extracellular domain (mutant) + hTGF-β2 - mouse
    
  • 1ks6 – cTGFBR-II extracellular domain - chicken
    
• TGF-β receptor III
  • 3qw9 – TGFBR-III ZP-C domain - rat
    
  • 4ajv – mTGFBR-III ZP-C domain
    
• TGF-β receptor I+II
  • 2pjy – hTGFBR-I extracellular domain (mutant) + hTGFBR-II extracellular domain (mutant) + TGF-β3
    
  • 3kfd – hTGFBR-I extracellular domain + hTGFBR-II extracellular domain + TGF-β1