| Description | The transforming growth factors-beta constitute a family of multi-functional cytokines that regulate cell growth and differentiation [ ]. Many cells synthesise TGF-beta, and essentially all have specific receptors for this peptide []. TGF-beta regulates the actions of many other peptide growth factors and determines a positive or negative direction of their effects.The complete amino acid sequence of human beta 2 transforming growth factor (hTGF-beta 2) has been determined by automated Edman degradation [ ]. Human TGF-beta 2 consists of 2 identical disulphide-linked subunits that share a high degree of similarity with the functionally related TGF-beta 1, and reveal lower levels of similarity to porcine inhibins and activins, the C-terminal regions of human Mullerian inhibiting substance, and the putative decapentaplegic gene complex protein of Drosophila melanogaster.The crystal structure of the TGF-beta 2 monomer lacks a well-defined hydrophobic core and displays an unusual elongated non-globular fold [ ]. Eight cysteine residues form 4 intra-chain disulphide bonds, creating the characteristic knotted arrangement. The dimer is stabilised by a ninth cysteine, which forms an inter-chain disulphide bond, and by 2 identical hydrophobic interfaces. Other members of the TGF-beta superfamily, including activins, inhibins and various developmental factors, are also likely to adopt the TGF-β fold. | Name | Transforming growth factor beta-2 proprotein |
| Short Name | TGFb2 | Type | Family |
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