TGF-beta receptor
From Proteopedia
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3D Structures of TGF-β receptor
Updated on 14-July-2015
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.
FunctionDiseaseOver-expression of TGF causes kidney disease, diabetes and renal disease. Mutations in TGFBR II cause various types of tumors. RelevanceStructural highlights | ||||||||||||
Updated on 14-July-2015
This page was last modified 10:08, 14 July 2015.