TGF-beta receptor: Difference between revisions

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Michal Harel, Alexander Berchansky, Jaime Prilusky

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 <StructureSection load='1ktz' size='340' side='right' caption='Human hTGFBR-II extracellular domain (green) complex with TGF-β3 (grey) (PDB code [[1ktz]])' scene=''>
-'''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.  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..  There are 3 types of TGFBR.  Both TGFBR I and II have high affinity for TGF-β1 and low affinity for TGF-β2.  TGFBR III has high affinity for TGF-β1, TGF-β2 and TGF-β1.2. <br />
-*'''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.<br />
-*'''TGFBR II''' is a tumor suppressor transmembrane protein.  <br />
-*'''TGFBR III''' is a cell-surface chondroitin sulfate / heparin sulfate proteoglycan.  It acts as a reservoir of ligand for TGFBRs.
 == 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.  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..  There are 3 types of TGFBR.     <br />
+*'''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. <br />
+*'''TGFBR II''' is a tumor suppressor transmembrane protein.  TGFBR II has high affinity for TGF-β1 and low affinity for TGF-β2. <br />
+*'''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.
-== Relevance ==
 == Structural highlights ==