TGF-beta receptor
From Proteopedia
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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=''> | <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. | ||
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== Function == | == 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 == | == Disease == | ||
Over-expression of TGF causes kidney disease, diabetes and renal disease. Mutations in TGFBR II cause various types of tumors. | Over-expression of TGF causes kidney disease, diabetes and renal disease. Mutations in TGFBR II cause various types of tumors. | ||
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| - | == Relevance == | ||
== Structural highlights == | == Structural highlights == | ||
Revision as of 06:59, 11 September 2016
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3D Structures of TGF-β receptor
Updated on 11-September-2016
