v5.1.0.3
Cicer data from the Legume Information System
Type | Family |
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 protein functions as a disulphide-linked homodimer. Its sequence is characterised by the presence of several C-terminal cysteine residues, which form interlocking disulphide links arranged in a knot-like topology. A similar "cystine-knot"arrangement has been noted in the structures of some enzyme inhibitors and neurotoxins that bind to voltage-gated Ca2+ channels, although the precise topology differs.The three-dimensional structures of several members of the TGF-beta super-family have been deduced [, , ]. TGF-beta genes are expressed differentially, suggesting that the various TGF-beta species may have distinct physiological roles in vivo. The solution structure of human TGF-beta 1 was determined using multinuclear magnetic resonance spectroscopy with hybrid distance geometry/simulated annealing [ ]. The structure shows a high degree of similarity to that of TGF-beta 2, but with notable differences in structure and flexibility. Examination of TGF-beta 1 mRNA levels in adult murine tissues indicates that expression is predominant in spleen, lung and placenta []. TGF-beta 1 is believed to play important roles in pathologic processes. |
Short Name | TGFb1 |