Solution structure of the chick TGFβ type II receptor ligand-binding domain

Journal of Molecular Biology

Volumn 326, Issue 4, 2003, Pages 989-997

  Marlow, Michael S ^a   Brown, Christopher B ^a,b   Barnett, Joey V ^a   Krezel, Andrzej M ^a  

^a VANDERBILT UNIVERSITY   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

Domain; Ligand binding; NMR; TGF ; Type II receptor

Indexed keywords

TRANSFORMING GROWTH FACTOR; TRANSFORMING GROWTH FACTOR BETA RECEPTOR;

ACIDITY; ARTICLE; CALCULATION; CARBON NUCLEAR MAGNETIC RESONANCE; CHICKEN; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENERGY; HUMAN; LIGAND BINDING; MOLECULAR INTERACTION; MOLECULAR MODEL; MOLECULAR RECOGNITION; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; RECEPTOR BINDING; SEQUENCE ANALYSIS; SIGNAL TRANSDUCTION; X RAY CRYSTALLOGRAPHY;

VERTEBRATA;

EID: 0037470580     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00023-8     Document Type: Article

References (40)

1. Massagué J. TGF-β signal transduction. Annu. Rev. Biochem. 67:1998;753-791.
2. Yamashita H., ten Dijke P., Franzen P., Miyazono K., Heldin C.H. Formation of hetero-oligomeric complexes of type I and type II receptors for transforming growth factor β J. Biol. Chem. 269:1994;20172-20178.
3. Wells R.G., Gilboa L., Sun Y., Liu X., Henis Y.I., Lodish H.F. Transforming growth factor-β induces formation of a dithiothreitol-resistant type I/Type II receptor complex in live cells. J. Biol. Chem. 274:1999;5716-5722.
4. Wrana J.L., Attisano L., Carcamo J., Zentella A., Doody J., Laiho M., et al. TGF-β signals through a heteromeric protein kinase receptor complex. Cell. 71:1992;1003-1014.
5. Wrana J.L., Attisano L., Wieser R., Ventura F., Massagué J. Mechanism of activation of the TGF-β receptor. Nature. 370:1994;341-347.
6. Abdollah S., Macias-Silva M., Tsukazaki T., Hayashi H., Attisano L., Wrana J.L. TβRI phosphorylation of Smad2 on Ser465 and Ser467 is required for Smad2-Smad4 complex formation and signaling. J. Biol. Chem. 272:1997;27678-27685.
7. Donovan J., Slingerland J. Transforming growth factor-beta and breast cancer: cell cycle arrest by transforming growth factor-β and its disruption in cancer. Breast Cancer Res. 2:2000;116-124.
8. Fortunel N.O., Hatzfeld A., Hatzfeld J.A. Transforming growth factor β: pleiotropic role in the regulation of hematopoiesis. Blood. 96:2000;2022-2036.
9. Bottner M., Krieglstein K., Unsicker K. The transforming growth factor-βs: structure, signaling, and roles in nervous system development and functions. J. Neurochem. 75:2000;2227-2240.
10. Letterio J.J., Roberts A.B. Regulation of immune responses by TGF-β Annu. Rev. Immunol. 16:1998;137-161.
11. Massagué J., Blain S.W., Lo R.S. TGF-β signaling in growth control, cancer, and heritable disorders. Cell. 103:2000;295-309.
12. McEarchern J.A., Kobie J.J., Mack V., Wu R.S., Meade-Tollin L., Arteaga C.L., et al. Invasion and metastasis of a mammary tumor involves TGF-β signaling. Int. J. Cancer. 91:2001;76-82.
13. George J., Roulot D., Koteliansky V.E., Bissell D.M. In vivo inhibition of rat stellate cell activation by soluble transforming growth factor β type II receptor: a potential new therapy for hepatic fibrosis. Proc. Natl Acad. Sci. USA. 96:1999;12719-12724.
14. Park J.A., Wang E., Kurt R.A., Schluter S.F., Hersh E.M., Akporiaye E.T. Expression of an antisense transforming growth factor-β1 transgene reduces tumorigenicity of EMT6 mammary tumor cells. Cancer Gene Ther. 4:1997;42-50.
15. Arteaga C.L., Hurd S.D., Winnier A.R., Johnson M.D., Fendly B.M., Forbes J.T. Anti-transforming growth factor TGF-β antibodies inhibit breast cancer cell tumorigenicity and increase mouse spleen natural killer cell activity. Implications for a possible role of tumor cell/host TGF-β interactions in human breast cancer progression. J. Clin. Invest. 92:1993;2569-2576.
16. Boesen C.C., Radaev S., Motyka S.A., Patamawenu A., Sun P.D. The 1.1 Å crystal structure of human TGF-β type II receptor ligand binding domain. Structure (Camb). 10:2002;913-919.
17. Greenwald J., Fischer W.H., Vale W.W., Choe S. Three-finger toxin fold for the extracellular ligand-binding domain of the type II activin receptor serine kinase. Nature Struct. Biol. 6:1999;18-22.
18. Hart P.J., Deep S., Taylor A.B., Shu Z., Hinck C.S., Hinck A.P. Crystal structure of the human TβR2 ectodomain-TGF-β3 complex. Nature Struct. Biol. 9:2002;203-208.
19. Kirsch T., Sebald W., Dreyer M.K. Crystal structure of the BMP-2-BRIA ectodomain complex. Nature Struct. Biol. 7:2000;492-496.
20. Barnett J.V., Moustakas A., Lin W., Wang X.F., Lin H.Y., Galper J.B., Maas R.L. Cloning and developmental expression of the chick type II and type III TGF-β receptors. Dev. Dynam. 199:1994;12-27.
21. Drenth J., Low B.W., Richardson J.S., Wright C.S. The toxin-agglutinin fold. A new group of small protein structures organized around a four-disulfide core. J. Biol. Chem. 255:1980;2652-2655.
22. Tsetlin V. Snake venom α-neurotoxins and other 'three-finger' proteins. Eur. J. Biochem. 264:1999;281-286.
23. ten Dijke P., Franzen P., Yamashita H., Ichijo H., Heldin C.-H., Miyazono K. Serine/threonine kinase receptors. Prog. Growth Factor Res. 5:1994;55-72.
24. Gray P.C., Greenwald J., Blount A.L., Kunitake K.S., Donaldson C.J., Choe S., Vale W. Identification of a binding site on the type II activin receptor for activin and inhibin. J. Biol. Chem. 275:2000;3206-3212.
25. Guimond A., Sulea T., Pepin M.C., O'Connor-McCourt M.D. Mapping of putative binding sites on the ectodomain of the type II TGF-β receptor by scanning-deletion mutagenesis and knowledge-based modeling. FEBS Letters. 456:1999;79-84.
26. Hinck A.P., Archer S.J., Qian S.W., Roberts A.B., Sporn M.B., Weatherbee J.A., et al. Transforming growth factor β1: three-dimensional structure in solution and comparison with the X-ray structure of transforming growth factor β 2. Biochemistry. 35:1996;8517-8534.
27. Mittl P.R., Priestle J.P., Cox D.A., McMaster G., Cerletti N., Grütter M.G. The crystal structure of TGF-β3 and comparison to TGF-β2: implications for receptor binding. Protein Sci. 5:1996;1261-1271.
28. Scheufler C., Sebald W., Hülsmeyer M. Crystal structure of human bone morphogenetic protein-2 at 2.7 Å resolution. J. Mol. Biol. 287:1999;103-115.
29. Jones S., Thornton J.M. Principles of protein-protein interactions. Proc. Natl Acad. Sci. USA. 93:1996;13-20.
30. 15N backbone assignments of the ligand binding domain of TGF-β type II receptor. J. Biomol. NMR. 17:2000;349-350.
31. Bartels C., Xia T., Billeter M., Güntert P., Wüthrich K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J. Biomol. NMR. 5:1995;1-10.
32. Güntert P., Mumenthaler C., Wüthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273:1997;283-298.
33. 1H nuclear magnetic resonance and distance geometry. J. Mol. Biol. 182:1985;295-315.
34. 15N enriched proteins. J. Am. Chem. Soc. 115:1993;7772-7777.
35. Clubb R.T., Ferguson S.B., Walsh C.T., Wagner G. Three-dimensional solution structure of Escherichia coli periplasmic cyclophilin. Biochemistry. 33:1994;2761-2772.
36. Cornilescu G., Delaglio F., Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR. 13:1999;289-302.
37. Bashford D., Case D.A. Generalized Born models of macromolecular solvation effects. Annu. Rev. Phys. Chem. 51:2000;129-152.
38. Xia B., Tsui V., Case D.A., Dyson H.J., Wright P.E. Comparison of protein solution structures refined by molecular dynamics simulation in vacuum, with a generalized Born model, and with explicit water. J. Biomol. NMR. 22:2002;317-331.
39. Kabsch W., Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 22:1983;2577-2637.
40. Laskowski R.A., Rullmannn J.A., MacArthur M.W., Kaptein R., Thornton J.M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR. 8:1996;477-486.