1m9z Citations

The 1.1 A crystal structure of human TGF-beta type II receptor ligand binding domain.

Structure 10 913-9 (2002)
Cited: 53 times
EuropePMC logo PMID: 12121646

Abstract

Transforming growth factor beta (TGF-beta) is involved in a wide range of biological functions including development, carcinogenesis, and immune regulation. Here we report the 1.1 A resolution crystal structure of human TGF-beta type II receptor ectodomain (TBRII). The overall structure of TBRII is similar to that of activin type II receptor ectodomain (ActRII) and bone morphogenic protein receptor type IA (BRIA). It displays a three-finger toxin fold with fingers formed by the beta strand pairs beta1-beta2, beta3-beta4, and beta5-beta6. The first finger in the TBRII is significantly longer than in ActRII and BRIA and folds tightly between the second finger and the C terminus. Surface charge distributions and hydrophobic patches predict potential TBRII binding sites.

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Reviews citing this publication (10)

  1. Mechanisms of TGF-beta signaling from cell membrane to the nucleus. Shi Y, Massagué J. Cell 113 685-700 (2003)
  2. Specificity and versatility in tgf-beta signaling through Smads. Feng XH, Derynck R. Annu Rev Cell Dev Biol 21 659-693 (2005)
  3. Structural Biology and Evolution of the TGF-β Family. Hinck AP, Mueller TD, Springer TA. Cold Spring Harb Perspect Biol 8 a022103 (2016)
  4. Molecular recognition in bone morphogenetic protein (BMP)/receptor interaction. Sebald W, Nickel J, Zhang JL, Mueller TD. Biol Chem 385 697-710 (2004)
  5. Intricacies of BMP receptor assembly. Nickel J, Sebald W, Groppe JC, Mueller TD. Cytokine Growth Factor Rev 20 367-377 (2009)
  6. Regulation of TGF-beta signalling by protein phosphatases. Liu T, Feng XH. Biochem J 430 191-198 (2010)
  7. Oligomeric interactions of TGF-β and BMP receptors. Ehrlich M, Gutman O, Knaus P, Henis YI. FEBS Lett 586 1885-1896 (2012)
  8. Design of growth factor sequestering biomaterials. Belair DG, Le NN, Murphy WL. Chem Commun (Camb) 50 15651-15668 (2014)
  9. Structural biology of the TGFβ family. Goebel EJ, Hart KN, McCoy JC, Thompson TB. Exp Biol Med (Maywood) 244 1530-1546 (2019)
  10. Transforming growth factor-β receptors: versatile mechanisms of ligand activation. Chia ZJ, Cao YN, Little PJ, Kamato D. Acta Pharmacol Sin 45 1337-1348 (2024)

Articles citing this publication (21)