Structural analysis of receptor tyrosine kinases

Progress in Biophysics and Molecular Biology

Volumn 71, Issue 3-4, 1999, Pages 343-358

  Hubbard, Stevan R ^a  

^a NEW YORK UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Growth factor receptor; Protein tyrosine kinase; Signal transduction; Tyrosine phosphorylation; X ray crystallography

Indexed keywords

ENDOTHELIAL CELL GROWTH FACTOR; LYMPHOKINE; PHOSPHOTYROSINE; PROTEIN TYROSINE KINASE; VASCULOTROPIN;

ANIMAL; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; DIMERIZATION; ENZYME ACTIVITY; ENZYME STRUCTURE; HUMAN; METABOLISM; PHOSPHORYLATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION; STRUCTURE ACTIVITY RELATION; X RAY CRYSTALLOGRAPHY;

ANIMALS; DIMERIZATION; ENDOTHELIAL GROWTH FACTORS; HUMANS; LYMPHOKINES; MODELS, MOLECULAR; PHOSPHORYLATION; PHOSPHOTYROSINE; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RECEPTOR PROTEIN-TYROSINE KINASES; VASCULAR ENDOTHELIAL GROWTH FACTOR A; VASCULAR ENDOTHELIAL GROWTH FACTORS;

ANIMALIA;

EID: 0032925147     PISSN: 00796107     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0079-6107(98)00047-9     Document Type: Article

References (67)

1. Banner D.W., D'Arcy A., Janes W., Gentz R., Schoenfeld H.J., Broger C., Loetscher H., Lesslauer W. Crystal structure of the soluble human 55 kd TNF receptor-human TNF beta complex: implications for TNF receptor activation. Cell. 73:1993;431-445.
2. Bargmann C.I., Hung M.C., Weinberg R.A. Multiple independent activations of the neu oncogene by a point mutation altering the transmembrane domain of p185. Cell. 45:1986;649-657.
3. Bellosta P., Costa M., Lin D.A., Basilico C. The receptor tyrosine kinase ARK mediates cell aggregation by homophilic binding. Mol. Cell. Biol. 15:1995;614-625.
4. 2+ adenylyl imidodiphosphate and inhibitor peptide PKI(5-24). EMBO J. 12:1993;849-859.
5. Burke C.L., Lemmon M.A., Coren B.A., Engelman D.M., Stern D.F. Dimerization of the p185neu transmembrane domain is necessary but not sufficient for transformation. Oncogene. 14:1997;687-696.
6. Cheon H.G., LaRochelle W.J., Bottaro D.P., Burgess W.H., Aaronson S.A. High-affinity binding sites for related fibroblast growth factor ligands reside within different receptor immunoglobulin-like domains. Proc. Natl. Acad. Sci. USA. 91:1994;989-993.
7. de Vos A.M., Ultsch M., Kossiakoff A.A. Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science. 255:1992;306-312.
8. DiGabriele A.D., Lax I., Chen D.I., Svahn C.M., Jaye M., Schlessinger J., Hendrickson W.A. Structure of a heparin-linked biologically active dimer of fibroblast growth factor. Nature. 393:1998;812-817.
9. Dikic I., Batzer A.G., Blaikie P., Obermeier A., Ullrich A., Schlessinger J., Margolis B. Shc binding to nerve growth factor receptor is mediated by the phosphotyrosine interaction domain. J. Biol. Chem. 270:1995;15125-15129.
10. Ellis L., Clauser E., Morgan D.O., Edery M., Roth R.A., Rutter W.J. Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose. Cell. 45:1986;721-732.
11. Flanagan J.G., Vanderhaeghen P. The ephrins and Eph receptors in neural development. Annu. Rev. Neurosci. 21:1998;309-345.
12. Garrett T.P.J., McKern N.M., Meizhen L., Frenkel M.J., Bentley J.D., Lovrecz G.O., Elleman T.C., Cosgrove L.J., Ward C.W. Crystal structure of the first three domains of the type-1 insulin-like growth factor receptor. Nature. 394:1998;395-399.
13. Gotoh N., Tojo A., Hino M., Yazaki Y., Shibuya M. A highly conserved tyrosine residue at codon 845 within the kinase domain is not required for the transforming activity of human epidermal growth factor receptor. Biochem. Biophys. Res. Commun. 186:1992;768-774.
14. Groenen L.C., Walker F., Burgess A.W., Treutlein H.R. A model for the activation of the epidermal growth factor receptor kinase: involvement of an asymmetric dimer? Biochemistry. 36:1997;3826-3836.
15. Hanks S.K., Quinn A.M., Hunter T. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science. 241:1991;42-52.
16. Heldin C.H. Dimerization of cell surface receptors in signal transduction. Cell. 80:1995;213-223.
17. Holland S.J., Peles E., Pawson T., Schlessinger J. Cell-contact-dependent signalling in axon growth and guid ance: Eph receptor tyrosine kinases and receptor protein tyrosine phosphatase beta. Curr. Opin. Neurobiol. 8:1998;117-127.
18. Hubbard S.R., Wei L., Ellis L., Hendrickson W.A. Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature. 372:1994;746-754.
19. Hubbard S.R. Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog. EMBO J. 16:1997;5572-5581.
20. Hubbard S.R., Mohammadi M., Schlessinger J. Autoregulatory mechanisms in protein-tyrosine kinases. J. Biol. Chem. 273:1998;11987-11990.
21. Isakoff S.J., Yu Y.P., Su Y.C., Blaikie P., Yajnik V., Rose E., Weidner K.M., Sachs M., Margolis B., Skolnik E.Y. Interaction between the phosphotyrosine binding domain of Shc and the insulin receptor is required for Shc phosphorylation by insulin in vivo. J. Biol. Chem. 271:1996;3959-3962.
22. Johnson L.N., Noble M.E.M., Owen D.J. Active and inactive protein kinases: structural basis for regulation. Cell. 85:1996;149-158.
23. Kato H., Faria T.N., Stannard B., Roberts C.T. Jr., LeRoith D. Essential role of tyrosine residues 1131, 1135 and 1136 of the insulin-like growth factor-I (IGF-I) receptor in IGF-I action. Mol. Endocrinol. 8:1994;40-50.
24. Lax I., Burgess W.H., Bellot F., Ullrich A., Schlessinger J., Givol D. Localization of a major receptor-binding domain for epidermal growth factor by affinity labeling. Mol. Cell. Biol. 8:1988;1831-1834.
25. Lemmon M.A., Bu Z., Ladbury J.E., Zhou M., Pinchasi D., Lax I., Engelman D.M., Schlessinger J. Two EGF molecules contribute additively to stabilization of the EGFR dimer. EMBO J. 16:1997;281-294.
26. Lemmon M.A., Pinchasi D., Zhou M., Lax I., Schlessinger J. Kit receptor dimerization is driven by bivalent binding of stem cell factor. J. Biol. Chem. 272:1997;6311-6317.
27. Levitzki A., Gazit A. Tyrosine kinase inhibition: an approach to drug development. Science. 267:1995;1782-1788.
28. Ling L., Templeton D., Kung H.J. Identification of the major autophosphorylation sites of Nyk/Mer, an NCAM-related receptor tyrosine kinase. J. Biol. Chem. 271:1996;18355-18362.
29. Livnah O., Stura E.A., Johnson D.L., Middleton S.A., Mulcahy L.S., Wrighton N.C., Dower W.J., Jolliffe L.K., Wilson I.A. Functional mimicry of a protein hormone by a peptide agonist: the EPO receptor complex at 2.8 Å Science. 273:1996;464-471.
30. Longati P., Bardelli A., Ponzetto C., Naldini L., Comoglio P.M. Tyrosines 1234-1235 are critical for activation of the tyrosine kinase encoded by the MET proto-oncogene (HGF receptor). Oncogene. 9:1994;49-57.
31. McCloskey P., Pierce J., Koski R.A., Varnum B., Liu E.T. Activation of the Axl receptor tyrosine kinase induces mitogenesis and transformation in 32D cells. Cell Growth Differ. 5:1994;1105-1117.
32. Middlemas D.S., Meisenhelder J., Hunter T. Identification of TrkB autophosphorylation sites and evidence that phospholipase C-γ 1 is a substrate of the TrkB receptor. J. Biol. Chem. 269:1994;5458-5466.
33. Mitra G. Mutational analysis of conserved residues in the tyrosine kinase domain of the human trk oncogene. Oncogene. 6:1991;2237-2241.
34. Mohammadi M., Dionne C.A., Li W., Li N., Spivak T., Honegger A.M., Jaye M., Schlessinger J. Point mutation in FGF receptor eliminates phosphatidylinositol hydrolysis without affecting mitogenesis. Nature. 358:1992;681-684.
35. Mohammadi M., Dikic I., Sorokin A., Burgess W.H., Jaye M., Schlessinger J. Identification of six novel autophosphorylation sites on fibroblast growth factor receptor 1 and elucidation of their importance in receptor activation and signal transduction. Mol. Cell. Biol. 16:1996;977-989.
36. Mohammadi M., Schlessinger J., Hubbard S.R. Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism. Cell. 86:1996;577-587.
37. Mohammadi M., McMahon G., Sun L., Tang C., Hirth P., Yeh B.K., Hubbard S.R., Schlessinger J. Structures of the tyrosine kinase domain of fibroblast growth factor receptor in complex with inhibitors. Science. 276:1997;955-960.
38. Mohammadi, M., Froum, S., Hamby, J.M., Schroeder, M.C., Panek, R.L., Liu, G.H., Eliseenkova, A.V., Green, D., Schlessinger, J., Hubbard, S.R., 1998. Crystal structure of an angiogenesis inhibitor bound to the FGF receptor tyrosine kinase domain. EMBO J. 17, 5896-5904.
39. Nakamura N., Chin H., Miyasaka N., Miura O. An epidermal growth factor receptor/Jak2 tyrosine kinase domain chimera induces tyrosine phosphorylation of Stat5 and transduces a growth signal in hematopoietic cells. J. Biol. Chem. 271:1996;19483-19488.
40. Nicholls A., Sharp K.A., Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins. 11:1991;281-296.
41. Obermeier A., Lammers R., Wiesmuller K.H., Jung G., Schlessinger J., Ullrich A. Identification of Trk binding sites for SHC and phosphatidylinositol 3′-kinase and formation of a multimeric signaling complex. J. Biol. Chem. 268:1993;22963-22966.
42. Pawson T. Protein modules and signalling networks. Nature. 373:1995;573-580.
43. 2+ flux but not mitogenesis. Nature. 358:1992;678-681.
44. Riedel H., Dull T.J., Schlessinger J., Ullrich A. A chimaeric receptor allows insulin to stimulate tyrosine kinase activity of epidermal growth factor receptor. Nature. 324:1986;68-70.
45. Roach P., Zick Y., Formisano P., Accili D., Taylor S.I., Gorden P. A novel human insulin receptor gene mutation uniquely inhibits insulin binding without impairing posttranslational processing. Diabetes. 43:1994;1096-1102.
46. Schreuder H., Tardif C., Trump-Kallmeyer S., Soffientini A., Sarubbi E., Akeson A., Bowlin T., Yanofsky S., Barrett R.W. A new cytokine-receptor binding mode revealed by the crystal structure of the IL-1 receptor with an antagonist. Nature. 386:1997;194-200.
47. Seedorf K., Felder S., Millauer B., Schlessinger J., Ullrich A. Analysis of platelet-derived growth factor receptor domain function using a novel chimeric receptor approach. J. Biol. Chem. 266:1991;12424-12431.
48. Sherrill J.M. Self-phosphorylation of epidermal growth factor receptor is an intermolecular reaction. Biochemistry. 36:1997;12890-12896.
49. Shoelson S.E., Chatterjee S., Chaudhuri M., White M.F. YMXM motifs of IRS-1 define substrate specificity of the insulin receptor kinase. Proc. Natl. Acad. Sci. USA. 89:1992;2027-2031.
50. Smith S.O., Smith C.S., Bormann B.J. Strong hydrogen bonding interactions involving a buried glutamic acid in the transmembrane sequence of the neu/erbB-2 receptor. Nat. Struct. Biol. 3:1996;252-258.
51. Spivak-Kroizman T., Lemmon M.A., Dikic I., Ladbury J.E., Pinchasi D., Huang J., Jaye M., Crumley G., Schlessinger J., Lax I. Heparin-induced oligomerization of FGF molecules is responsible for FGF receptor dimerization, activation and cell proliferation. Cell. 79:1994;1015-1024.
52. Stephens R.M., Loeb D.M., Copeland T.D., Pawson T., Greene L.A., Kaplan D.R. Trk receptors use redundant signal transduction pathways involving SHC and PLC-gamma 1 to mediate NGF responses. Neuron. 12:1994;691-705.
53. Sternberg M.J., Gullick W.J. Neu receptor dimerization. Nature. 339:1989;587.
54. Stetefeld J., Mayer U., Timpl R., Huber R. Crystal structure of three consecutive laminin-type epidermal growth factor-like (LE) modules of laminin gamma1 chain harboring the nidogen binding site. J. Mol. Biol. 257:1996;644-657.
55. Taylor S.T., Radzio-Andzelm E. Three protein kinase structures define a common motif. Structure. 2:1994;345-355.
56. Taylor S.S., Radzio-Andzelm E., Hunter T. How do protein kinases discriminate between serine/threonine and tyrosine? Stuctural insights from the insulin receptor protein-tyrosine kinase. FASEB J. 9:1995;1255-1266.
57. Ueno H., Hirano N., Kozutsumi H., Sasaki K., Tanaka T., Yazaki Y., Hirai H. An epidermal growth factor receptor-leukocyte tyrosine kinase chimeric receptor generates ligand-dependent growth signals through the Ras signaling pathway. J. Biol. Chem. 270:1995;20135-20142.
58. Ullrich A., Schlessinger J. Signal transduction by receptors with tyrosine kinase activity. Cell. 61:1990;203-212.
59. Walter M.R., Windsor W.T., Nagabhushan T.L., Lundell D.J., Lunn C.A., Zauodny P.J., Narula S.K. Crystal structure of a complex between interferon-γ and its soluble high-affinity receptor. Nature. 376:1995;230-235.
60. Wei L., Hubbard S.R., Hendrickson W.A., Ellis L. Expression, characterization, and crystallization of the catalytic core of the human insulin receptor protein-tyrosine kinase domain. J. Biol. Chem. 270:1995;8122-8130.
61. Wiesmann C., Fuh G., Christinger H.W., Eigenbrot C., Wells J.A., de Vos A.M. Crystal structure at 1.7 Å resolution of VEGF in complex with domain 2 of the Flt-1 receptor. Cell. 91:1997;695-704.
62. Wilden P.A., Kahn C.R., Siddle K., White M.F. Insulin receptor kinase domain autophosphorylation regulates receptor enzymatic function. J. Biol. Chem. 267:1992;16660-16668.
63. Xiong Q., Chan J.L., Zong C.S., Wang L.H. Two chimeric receptors of epidermal growth factor receptor and c-Ros that differ in their transmembrane domains have opposite effects on cell growth. Mol. Cell. Biol. 16:1996;1509-1518.
64. Yamaguchi H., Hendrickson W.A. Structural basis for activation of the human lymphocyte kinase Lck upon tyrosine phosphorylation. Nature. 384:1996;484-489.
65. Zheng J., Knighton D.R., Ten Eyck L.F., Karlsson R.K., Xuong N.H., Taylor S.S., Sowadski J.M. Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor. Biochemistry. 32:1993;2154-2161.
66. Zhou S., Carraway K.L. III, Eck M.J., Harrison S.C., Feldman R.A., Mohammadi M., Schlessinger J., Hubbard S.R., Smith D.P., Eng C., Lorenzo M.J., Ponder B.A.J., Mayer B.J., Cantley L.C. Catalytic specificity of protein-tyrosine kinases is critical for selective signalling. Nature. 373:1995;536-539.
67. Zong C.S., Chan J.L.K., Yang S.K., Wang L.H. Mutations of Ros differentially effecting signal transduction pathways leading to cell growth versus transformation. J. Biol. Chem. 272:1997;1500-1506.