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Transforming growth factor beta like domain
Identifiers
Symbol TGF_beta
Pfam PF00019
InterPro IPR001839
PROSITE PDOC00223
SCOP 1tfg

The transforming growth factor beta (TGF-β) superfamily is a large family of structurally related cell regulatory proteins that was named after its first member, TGF-β1, originally described in 1983[1].

Many proteins have since been described as members of the TGF-β superfamily in a variety of species, including invertebrates as well as vertebrates and categorized into 23 distinct gene types that fall into four major subfamilies:[2] [3][4].

  • the TGF-β subfamily
  • a group encompassing various divergent members

Transforming growth factor-beta (TGF-beta)[5] is a multifunctional peptide that controls proliferation, differentiation and other functions in many cell types. TGF-beta-1 is a peptide of 112 amino acid residues derived by proteolytic cleavage from the C-terminal of a precursor protein.

These molecules interact with a conserved family of cell surface serine/threonine-specific protein kinase receptors, and generate intracellular signals using a conserved family of proteins called SMADs. They play fundamental roles in the regulation of basic biological processes such as growth, development, tissue homeostasis and regulation of the immune system.[2]

Structure

Proteins from the TGF-beta family are only active as homo- or heterodimer; the two chains being linked by a single disulfide bond. From X-ray studies of TGF-beta-2[6], it is known that all the other cysteines are involved in intrachain disulfide bonds. As shown in the following schematic representation, there are four disulfide bonds in the TGF-beta's and in inhibin beta chains, while the other members of this family lack the first bond.

                                                     interchain
                                                     |
          +------------------------------------------|+
          |                                          ||
xxxxcxxxxxCcxxxxxxxxxxxxxxxxxxCxxCxxxxxxxxxxxxxxxxxxxCCxxxxxxxxxxxxxxxxxxxCxCx
    |      |                  |  |                                        | |
    +------+                  +--|----------------------------------------+ |
                                 +------------------------------------------+

'C': conserved cysteine involved in a disulfide bond.

Human proteins containing this domain

AMH; ARTN; BMP10; BMP15; BMP2; BMP3; BMP4; BMP5; BMP6; BMP7; BMP8A; BMP8B; GDF1; GDF10; GDF11; GDF15; GDF2; GDF3; GDF3A; GDF5; GDF6; GDF7; GDF8; GDF9; GDNF; INHA; INHBA; INHBB; INHBC; INHBE; LEFTY1; LEFTY2; MSTN; NODAL; NRTN; PSPN; TGFB1; TGFB2; TGFB3;

References

  1. ^ Assoian R, Komoriya A, Meyers C, Miller D, Sporn M (1983). "Transforming growth factor-beta in human platelets. Identification of a major storage site, purification, and characterization". J Biol Chem 258 (11): 7155–60. PMID 6602130.  
  2. ^ a b Herpin A, Lelong C, Favrel P (2004). "Transforming growth factor-beta-related proteins: an ancestral and widespread superfamily of cytokines in metazoans". Dev Comp Immunol 28 (5): 461–85. doi:10.1016/j.dci.2003.09.007. PMID 15062644.  
  3. ^ Burt DW (1992). "Evolutionary grouping of the transforming growth factor-beta superfamily". Biochem. Biophys. Res. Commun. 184 (2): 590–595. doi:10.1016/0006-291X(92)90630-4. PMID 1575734.  
  4. ^ Burt DW, Law AS (1994). "Evolution of the transforming growth factor-beta superfamily". Prog. Growth Factor Res. 5 (1): 99–118. doi:10.1016/0955-2235(94)90020-5. PMID 8199356.  
  5. ^ Roberts AB, Sporn MB (1990). Peptide growth factors and their receptors. pp. 419–475. ISBN 35-405-118-49.  
  6. ^ Davies DR, Daopin S, Piez KA, Ogawa Y (1992). "Crystal structure of transforming growth factor-beta 2: an unusual fold for the superfamily". Science 257 (5068): 369–373. doi:10.1126/science.1631557. PMID 1631557.  
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