Transforming growth factor beta superfamily
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| Transforming growth factor beta like domain
| ||
| Identifiers | ||
| Symbol | TGF_beta | |
| Pfam | PF00019 | |
| InterPro | IPR001839 | |
| SCOP | 1tfg | |
| Available PDB structures:
1ktzA:312-412 1tgjA:312-412 1tgk :312-412 1tfg :314-414 2tgi :314-414 1kldA:290-390 1klcB:290-390 1klaA:290-390 1nyuB:318-426 1nysD:318-426 2b0uB:318-426 1s4yD:318-426 1m4uL:327-431 1bmp :328-431 1lxiA:327-431 1lx5A:327-431 1es7A:293-396 1rewB:293-396 1reuA:294-396 3bmpA:293-396 2bhkA:397-501 1waqA:397-501 1zkzA:324-429 1ehuA:290-393 1ehrA:290-393 1agqB:115-211 | ||
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:[1] [1][1].
- the decapentaplegic-Vg-related (DVR) related subfamily (including the bone morphogenetic proteins and the growth differentiation factors)
- the TGF-β subfamily
- a group encompassing various divergent members
Transforming growth factor-beta (TGF-beta)[1] 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.[1]
Structure
Proteins from the TGF-beta family are only active as homo- or heterodimer; the two chains being linked by a single disulphide bond. From X-ray studies of TGF-beta-2[1], it is known that all the other cysteines are involved in intrachain disulphide bonds. As shown in the following schematic representation, there are four disulphide 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 disulphide 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
Cell signaling: TGF beta signaling pathway | |
|---|---|
| TGF beta superfamily of ligands | TGF beta family (TGF-β1, TGF-β2, TGF-β3) Bone morphogenetic proteins (BMP2, BMP3, BMP4, BMP5, BMP6, BMP7, BMP8a, BMP8b, BMP10 , BMP15) Growth differentiation factors (GDF1, GDF2, GDF3, GDF5, GDF6, GDF7, Myostatin/GDF8, GDF9, GDF10, GDF11, GDF15) Other (Activin A and B/Inhibin A and B, Anti-müllerian hormone, Nodal) |
| TGF beta receptors | TGFBR1: Activin type 1 receptors (ACVR1, ACVR1B, ACVR1C) - ACVRL1 - BMPR1 (BMPR1A - BMPR1B) TGFBR2: Activin type 2 receptors (ACVR2A, ACVR2B) - AMHR2 - BMPR2 TGFBR3: betaglycan |
| Transducers/SMAD | R-SMAD (SMAD1, SMAD2, SMAD3, SMAD5, SMAD9) - I-SMAD (SMAD6, SMAD7) - SMAD4 |
| Ligand Inhibitors | Cerberus - Chordin - DAN - Decorin - Follistatin - Gremlin - Lefty - LTBP1 - Noggin - THBS1 |
| Coreceptors | BAMBI - Cripto |
| Other | SARA |
