F
IPR003940

Transforming growth factor beta-2 proprotein

InterPro entry
Short nameTGFb2
family relationships

Description

The transforming growth factors-beta constitute a family of multi-functional cytokines that regulate cell growth and differentiation
[2]
. Many cells synthesise TGF-beta, and essentially all have specific receptors for this peptide
[3]
. 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
[3]
. 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
[1]
. 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.

References

1.Crystal structure of transforming growth factor-beta 2: an unusual fold for the superfamily. Daopin S, Piez KA, Ogawa Y, Davies DR. Science 257, 369-73, (1992). View articlePMID: 1631557

2.Transforming growth factor beta 1: NMR signal assignments of the recombinant protein expressed and isotopically enriched using Chinese hamster ovary cells. Archer SJ, Bax A, Roberts AB, Sporn MB, Ogawa Y, Piez KA, Weatherbee JA, Tsang ML, Lucas R, Zheng BL. Biochemistry 32, 1152-63, (1993). View articlePMID: 8424942

3.The transforming growth factor-beta system, a complex pattern of cross-reactive ligands and receptors. Cheifetz S, Weatherbee JA, Tsang ML, Anderson JK, Mole JE, Lucas R, Massague J. Cell 48, 409-15, (1987). View articlePMID: 2879635

Further reading

4. The crystal structure of TGF-beta 3 and comparison to TGF-beta 2: implications for receptor binding. Mittl PR, Priestle JP, Cox DA, McMaster G, Cerletti N, Grutter MG. Protein Sci. 5, 1261-71, (1996). View articlePMID: 8819159

5. Transforming growth factor beta 1: three-dimensional structure in solution and comparison with the X-ray structure of transforming growth factor beta 2. Hinck AP, Archer SJ, Qian SW, Roberts AB, Sporn MB, Weatherbee JA, Tsang ML, Lucas R, Zhang BL, Wenker J, Torchia DA. Biochemistry 35, 8517-34, (1996). View articlePMID: 8679613

GO terms

biological process

  • None

cellular component

  • None
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