Efficiency of signalling through cytokine receptors depends critically on receptor orientation

Nature

Volumn 395, Issue 6701, 1998, Pages 511-516

  Syed, Rashid S ^a   Reid, Scott W ^b   Li, Cuiwei ^a   Cheetham, Janet C ^a   Aoki, Kenneth H ^a   Liu, Beishan ^b   Zhan, Hangjun ^b   Osslund, Timothy D ^a   Chirino, Arthur J ^a   Zhang, Jiandong ^a   Finer Moore, Janet ^c   Elliott, Steven ^a   Sitney, Karen ^a   Katz, Bradley A ^b   Matthews, David J ^b   Wendoloski, John J ^a   Egrie, Joan ^a   Stroud, Robert M ^b,c  

^a AMGEN INC   (United States)

^b Axys Pharmaceuticals Inc   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ERYTHROPOIETIN; ERYTHROPOIETIN RECEPTOR;

AMINO ACID SEQUENCE; ARTICLE; CRYSTAL STRUCTURE; PRIORITY JOURNAL; RECEPTOR BINDING; SIGNAL TRANSDUCTION;

CRYSTALLOGRAPHY, X-RAY; ERYTHROPOIETIN; ESCHERICHIA COLI; HUMAN GROWTH HORMONE; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PICHIA; PROTEIN CONFORMATION; RECEPTORS, ERYTHROPOIETIN; RECOMBINANT PROTEINS; SIGNAL TRANSDUCTION; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0032188942     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/26773     Document Type: Article

References (29)

1. Graber, S. E. & Krantz, S. B. Erythropoietin and the control of red blood cell production. Annu. Rev. Med. 29, 51-66 (1978).
2. Damen, J. E. & Krystal, G. Early events in erythropoietin-induced signaling. Exp. Hematol. 24, 1455-1459 (1996).
3. Johnson, D. L. et al. Identification of a 13 amino acid peptide mimetic of erythropoietin and description of amino acids critical for the mimetic activity of EMP1. Biochemistry 37, 3699-3710 (1998).
4. Philo, J. S., Aoki, K. H., Arakawa, T., Narhi, L. O. & Wen, J. Dimerization of the extracellular domain of the erythropoietin (EPO) receptor by EPO: one high-affinity and one low-affinity interaction. Biochemistry 35, 1681-1691 (1996).
5. Wrighton, N. C. et al. Small peptides as potent mimetics of the protein hormone erythropoietin. Science 273, 458-464 (1996).
6. Livnah, O. et al. Functional mimicry of a protein hormone by a peptide agonist: the EPO receptor complex at 2.8 Å. Science 273, 464-471 (1996).
7. Derby, P., Aoki, K. H., Katta, V. & Rohde, M. F. in Techniques in Protein Chemistry VII (ed. Marshak, D. R.) 109-119 (Academic, San Diego, 1996).
8. Hilton, D. J., Watowich, S. S., Katz, L. & Lodish, H. F. Saturation mutagenesis of the WSXWS motif of the erythropoietin receptor. J. Biol. Chem. 271, 4699-4708 (1996).
9. Abrahams, J. P. & Leslie, A. G. W. Acta Crystallogr. D 52, 30-42 (1996).
10. Cheetham, J. C. et al. NMR structure of human erythropoietin and a comparison with its receptor bound conformation. Nature Struct. Biol. (in the press).
11. De Vos, A. M., Ultsch, M. & Kossiakoff, A. A. Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science 255, 306-312 (1992).
12. Sprang, S. R. & Bazan, J. F. Cytokine structural taxonomy and mechanisms of receptor engagement. Curr. Opin. Struct. Biol. 3, 815-827 (1993).
13. Rozwarski, D. A. et al. Structural comparisons among the short-chain helical cytokines. Structure 2, 159-173 (1994).
14. Yoshimura, A. et al. Mutations in the Trp-Ser-X-Trp-Ser motif of the erythropoietin receptor abolish processing, ligand binding, and activation of the receptor. J. Biol. Chem. 267, 11619-11625 (1992).
15. Baumgartner, J. W., Wells, C. A., Chen, C. M. & Waters, M. J. The role of the WSXWS equivalent motif in growth-hormone receptor function. J. Biol. Chem. 269, 29094-29101 (1994).
16. Barbone, F. P. et al. Mutagenesis studies of the human erythropoietin receptor. Establishment of structure-function relationships. J. Biol. Chem. 272, 4985-4992 (1997).
17. Middleton, S. A. et al. Identification of a critical ligand-binding determinant of the human erythropoietin receptor - evidence for common ligand-binding motifs in the cytokine receptor family. J. Biol. Chem. 271, 14045-14054 (1996).
18. Grodberg, J., Davis, K. L. & Sykowski, A. J. Alanine scanning mutagenesis of human erythropoietin identifies four amino acids which are critical for biological activity. Eur. J. Biochem. 218, 597-601 (1993).
19. Wen, D. Y., Boissel, J. P., Showers, M., Ruch, B. C. & Bunn, H. F. Erythropoietin structure-function relationships-identification of functionally important domains. J. Biol. Chem. 269, 22839-22846 (1994).
20. Matthews, D. J., Topping, R. S., Cass, R. T. & Giebel, L. B. A sequential dimerization mechanism for erythropoietin receptor activation. Proc. Natl Acad. Sci. USA 93, 9471-9476 (1996).
21. Elliott, S., Lorenzini, T., Chang, D., Barzilay, J. & Delorme, E. Mapping of the active site of recombinant human erythropoietin. Blood 89, 493-502 (1997).
22. Clackson, T. & Wells, J. A. A hot spot of binding energy in a hormone-receptor interface. Science 267, 383-386 (1995).
23. Watowich, S. S. et al. Homodimerization and constitutive activation of the erythropoietin receptor. Proc. Natl Acad. Sci. USA 89, 2140-2144 (1992).
24. Narhi, L. O. et al. The effect of carbohydrate on the structure and stability of erythropoietin. J. Biol. Chem. 266, 23022-23026 (1991).
25. Johnson, D. L. et al. Refolding, purification, and characterization of human erythropoietin binding protein produced in Escherichia coli. Prot. Express. Purif. 7, 104-113 (1996).
26. Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
27. Collaborative Computational Project No. 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
28. Brunger, A. T. X-PLOR, Version 3.1, A System for X-ray Crystallography and NMR (Yale Univ. Press, New Haven, 1992).
29. Furey, W. & Swaminathan, S. Phases-95: a program package for processing and analyzing diffraction data from macromolecules. Methods Enzymol. 277, 590-620 (1997).