|PROSITE documentation PDOC51364 [for PROSITE entry PS51364]|
Transforming growth factor β family of cytokines, are potent and multifunctional signaling molecules (see <PDOC00223>). Prior to ligand receptor binding there exist extracellular regulators that target these cytokines and facilitate the formation of morphogen gradiants that control developmental processes. Some of these proteins that are known to sequester latent TGF-β contains a conserved domain, the TGF-β binding (TB) domain. It is characterised by 8 conserved cysteine residues, which include an unusual cysteine triplet [1,2].
The TB fold is globular with six β-strands and two α-helices (see <PDB:1APJ>) [1,2,3]. The pairing of the eight cysteines is 1-3, 2-6, 4-7, and 5-8, creating a fairly rigid structure. In follistatin and in the first repeat of fibrillin and LTBPs the last disulfide bridge is absent.
The proteins that contain a TB domain are listed below:
The profile we developed covers the whole TB domain.Last update:
January 2008 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Yuan X. Downing A.K. Knott V. Handford P.A.|
|Title||Solution structure of the transforming growth factor beta-binding protein-like module, a domain associated with matrix fibrils.|
|Source||EMBO J. 16:6659-6666(1997).|
|2||Authors||Lack J. O'Leary J.M. Knott V. Yuan X. Rifkin D.B. Handford P.A. Downing A.K.|
|Title||Solution structure of the third TB domain from LTBP1 provides insight into assembly of the large latent complex that sequesters latent TGF-beta.|
|Source||J. Mol. Biol. 334:281-291(2003).|
|3||Authors||Lee S.S. Knott V. Jovanovic J. Harlos K. Grimes J.M. Choulier L. Mardon H.J. Stuart D.I. Handford P.A.|
|Title||Structure of the integrin binding fragment from fibrillin-1 gives new insights into microfibril organization.|
|4||Authors||Thompson T.B. Lerch T.F. Cook R.W. Woodruff T.K. Jardetzky T.S.|
|Title||The structure of the follistatin:activin complex reveals antagonism of both type I and type II receptor binding.|
|Source||Dev. Cell 9:535-543(2005).|