메뉴 건너뛰기




Volumn 4, Issue 6, 1997, Pages 498-504

Solution structure of an extracellular domain containing the WSxWS motif of the granulocyte colony-stimulating factor receptor and its interaction with ligand

Author keywords

[No Author keywords available]

Indexed keywords

GRANULOCYTE COLONY STIMULATING FACTOR; GROWTH FACTOR RECEPTOR;

EID: 0031005782     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0697-498     Document Type: Article
Times cited : (31)

References (48)
  • 1
    • 0024384630 scopus 로고
    • Hematopoietic cell growth factors and their receptors
    • Nicola, N.A. Hematopoietic cell growth factors and their receptors. Annu. Rev. Biochem. 58, 45-77 (1989).
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 45-77
    • Nicola, N.A.1
  • 2
    • 0025162844 scopus 로고
    • Structural design and molecular evolution of a cytokine receptor superfamily
    • Bazan J.F. Structural design and molecular evolution of a cytokine receptor superfamily. Proc. Natl. Acad. Sci. USA 87, 6934-6938 (1990).
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6934-6938
    • Bazan, J.F.1
  • 4
    • 0028117163 scopus 로고
    • Cytokine signal transduction
    • Kishimoto, T., Taga, T. & Akira, S. Cytokine signal transduction. Cell 76, 253-262 (1994).
    • (1994) Cell , vol.76 , pp. 253-262
    • Kishimoto, T.1    Taga, T.2    Akira, S.3
  • 5
    • 0025895320 scopus 로고
    • Neuropoietic cytokines in the hematopoietic fold
    • Bazan, J.F. Neuropoietic cytokines in the hematopoietic fold. Neuron 7, 197-208 (1991).
    • (1991) Neuron , vol.7 , pp. 197-208
    • Bazan, J.F.1
  • 6
    • 0025270168 scopus 로고
    • Expression and cloning of a receptor for murine granulocyte colony-stimulating factor
    • Fukunaga, R., Ishizaka-Ikeda, E., Seto, Y. & Nagata, S. Expression and cloning of a receptor for murine granulocyte colony-stimulating factor. Cell 61, 341-350 (1990).
    • (1990) Cell , vol.61 , pp. 341-350
    • Fukunaga, R.1    Ishizaka-Ikeda, E.2    Seto, Y.3    Nagata, S.4
  • 7
    • 0025861158 scopus 로고
    • Functional domains of the granulocyte colony-stimulating factor receptor
    • Fukunaga, R., Ishizaka-Ikeda, E., Pan, C.-X., Seto, Y. & Nagata, S. Functional domains of the granulocyte colony-stimulating factor receptor. EMBO J. 10, 2855-2865 (1991).
    • (1991) EMBO J. , vol.10 , pp. 2855-2865
    • Fukunaga, R.1    Ishizaka-Ikeda, E.2    Pan, C.-X.3    Seto, Y.4    Nagata, S.5
  • 8
    • 0026332810 scopus 로고
    • Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule
    • Cunningham, B.C., Ultsch, M., De Vos, A.M., Mulkerrin, M.G., Clauser, K.R. & Wells J.A. Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule. Science 254, 832-825 (1991).
    • (1991) Science , vol.254 , pp. 832-1825
    • Cunningham, B.C.1    Ultsch, M.2    De Vos, A.M.3    Mulkerrin, M.G.4    Clauser, K.R.5    Wells, J.A.6
  • 9
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • De Vos, A.M., Ultsch, M. & Kossiakoff, A.A. Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science 236, 306-312 (1992).
    • (1992) Science , vol.236 , pp. 306-312
    • De Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 10
    • 0028843914 scopus 로고
    • Requirement for the immunoglobulin-like domain of granulocyte colony-stimulating factor receptor in formation of a 2:1 receptor-ligand complex
    • Hiraoka, O., Anaguchi, H., Asakura, A & Ota, Y. Requirement for the immunoglobulin-like domain of granulocyte colony-stimulating factor receptor in formation of a 2:1 receptor-ligand complex. J. Biol. Chem. 270, 25928-25934 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 25928-25934
    • Hiraoka, O.1    Anaguchi, H.2    Asakura, A.3    Ota, Y.4
  • 11
    • 0027258762 scopus 로고
    • The structure of granulocyte-colony-stimulating factor and its relationship to other growth factors
    • Hill, C.P., Osslund, T.D. & Eisenberg, D. The structure of granulocyte-colony-stimulating factor and its relationship to other growth factors. Proc. Natl. Acad. Sci. USA 90, 5167-5171 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5167-5171
    • Hill, C.P.1    Osslund, T.D.2    Eisenberg, D.3
  • 12
    • 0027989744 scopus 로고
    • Structure and dynamics of the human granulocyte colony-stimulating factor determined by NMR spectroscopy. Loop mobility in a four-helix-bundle protein
    • Zink, T., Ross, A., Lüers, K., Cieslar, C., Rudolph R. & Holak T.A. Structure and dynamics of the human granulocyte colony-stimulating factor determined by NMR spectroscopy. Loop mobility in a four-helix-bundle protein. Biochemistry, 33, 8453-8463 (1994)
    • (1994) Biochemistry , vol.33 , pp. 8453-8463
    • Zink, T.1    Ross, A.2    Lüers, K.3    Cieslar, C.4    Rudolph, R.5    Holak, T.A.6
  • 13
    • 0028247007 scopus 로고
    • Secondary structure and backbone dynamics of human granulocyte colony-stimulating factor in solution
    • Werner, J.M. et al. Secondary structure and backbone dynamics of human granulocyte colony-stimulating factor in solution. Biochemistry 33, 7184-7192 (1994).
    • (1994) Biochemistry , vol.33 , pp. 7184-7192
    • Werner, J.M.1
  • 14
  • 15
    • 0028825115 scopus 로고
    • Ligand binding characteristics of the carboxyl-terminal domain of the cytokine receptor homologous region of the granulocyte colony-stimulating factor receptor
    • Anaguchi, H., Hiraoka, O., Yamasaki, K., Naito, S. & Ota, Y. Ligand binding characteristics of the carboxyl-terminal domain of the cytokine receptor homologous region of the granulocyte colony-stimulating factor receptor. J. Biol. Chem. 270, 27845-27851 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 27845-27851
    • Anaguchi, H.1    Hiraoka, O.2    Yamasaki, K.3    Naito, S.4    Ota, Y.5
  • 17
    • 0026496886 scopus 로고
    • The three-dimensional structure of the tenth type III module of fibronectin: An insight into RGD-mediated interactions
    • Main, A.L., Harvey, T.S., Baron, M., Boyd, J. & Campbell, I.D. The three-dimensional structure of the tenth type III module of fibronectin: an insight into RGD-mediated interactions. Cell 71, 671-678 (1992).
    • (1992) Cell , vol.71 , pp. 671-678
    • Main, A.L.1    Harvey, T.S.2    Baron, M.3    Boyd, J.4    Campbell, I.D.5
  • 18
    • 0026490256 scopus 로고
    • Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein
    • Leahy, D. J., Hendricson, W.A., Aukhil, I. & Erickson, H.P. Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein. Science 258, 987-991 (1992).
    • (1992) Science , vol.258 , pp. 987-991
    • Leahy, D.J.1    Hendricson, W.A.2    Aukhil, I.3    Erickson, H.P.4
  • 19
    • 0028032203 scopus 로고
    • The X-ray structure of a growth hormone-prolactin receptor complex
    • Sommers, W., Ultsch, M., De Vos, A.M. & Kossiakoff, A.A. The X-ray structure of a growth hormone-prolactin receptor complex. Nature 372, 478-481 (1994).
    • (1994) Nature , vol.372 , pp. 478-481
    • Sommers, W.1    Ultsch, M.2    De Vos, A.M.3    Kossiakoff, A.A.4
  • 20
    • 0029067876 scopus 로고
    • Crystal structure of a complex between interferon-g and its soluble high-affinity receptor
    • Walter, M.R. et al. Crystal structure of a complex between interferon-g and its soluble high-affinity receptor. Nature 376, 230-235 (1995).
    • (1995) Nature , vol.376 , pp. 230-235
    • Walter, M.R.1
  • 21
    • 0025198478 scopus 로고
    • Atomic structure of a fragment of human CD4 containing two immunoglobulin-like domains
    • Wang, J.-H. et al. Atomic structure of a fragment of human CD4 containing two immunoglobulin-like domains. Nature 348, 411-418 (1990).
    • (1990) Nature , vol.348 , pp. 411-418
    • Wang, J.-H.1
  • 22
    • 0025224767 scopus 로고
    • Crystal structure of an HIV-binding recombinant fragment of human CD4
    • Ryu, S.-E. et al. Crystal structure of an HIV-binding recombinant fragment of human CD4. Nature 348, 419-426 (1990).
    • (1990) Nature , vol.348 , pp. 419-426
    • Ryu, S.-E.1
  • 23
    • 0024468229 scopus 로고
    • Crystal structure of chaperone protein Pap D reveals an immunoglobulin fold
    • Holmgren, A. & Bränden, C.I. Crystal structure of chaperone protein Pap D reveals an immunoglobulin fold. Nature 342, 248 (1989).
    • (1989) Nature , vol.342 , pp. 248
    • Holmgren, A.1    Bränden, C.I.2
  • 24
    • 0029798402 scopus 로고    scopus 로고
    • Functional mimicry of a protein hormone by a peptide agonist: The EPO receptor complex at 2.8
    • Livnah, O. et al. Functional mimicry of a protein hormone by a peptide agonist: the EPO receptor complex at 2.8. Science 273, 464-471 (1996).
    • (1996) Science , vol.273 , pp. 464-471
    • Livnah, O.1
  • 25
    • 0025942918 scopus 로고
    • The integrity of the conserved 'WS motif' common to IL-2 and other cytokine receptors is essential for ligand binding and signal transduction
    • Miyazaki, T., Maruyama, M., Yamada, G., Hatakeyama, M. & Taniguchi, T. The integrity of the conserved 'WS motif' common to IL-2 and other cytokine receptors is essential for ligand binding and signal transduction. EMBO J. 10, 3191-3197 (1991).
    • (1991) EMBO J. , vol.10 , pp. 3191-3197
    • Miyazaki, T.1    Maruyama, M.2    Yamada, G.3    Hatakeyama, M.4    Taniguchi, T.5
  • 26
    • 0027467218 scopus 로고
    • Structure-function analysis of human IL-6 receptor: Dissociation of amino acid residues required for IL-6-binding and for IL-6 signal transduction through gp130
    • Yawata, H. et al. Structure-function analysis of human IL-6 receptor: dissociation of amino acid residues required for IL-6-binding and for IL-6 signal transduction through gp130. EMBOJ. 12, 1705-1712 (1993).
    • (1993) EMBOJ. , vol.12 , pp. 1705-1712
    • Yawata, H.1
  • 27
    • 0026643982 scopus 로고
    • Mutations in the Trp-Ser-X-Trp-Ser motif of the erythropoietin receptor abolish processing, ligand binding, and activation of the receptor
    • 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).
    • (1992) J. Biol. Chem. , vol.267 , pp. 11619-11625
    • Yoshimura, A.1
  • 28
    • 0025630163 scopus 로고
    • Molecular cloning and expression of an IL-6 signal transducer, gp130
    • Hibi, M. et al. Molecular cloning and expression of an IL-6 signal transducer, gp130. Cell 63, 1149-1157 (1990).
    • (1990) Cell , vol.63 , pp. 1149-1157
    • Hibi, M.1
  • 29
    • 0028822206 scopus 로고
    • The evolution of hematopoietic cytokine/receptor complexes
    • Shields, D.C., Harmon, D.L., Nunez, F., & Whitehead, A.S. The evolution of hematopoietic cytokine/receptor complexes. Cytokine 7, 679-688 (1995).
    • (1995) Cytokine , vol.7 , pp. 679-688
    • Shields, D.C.1    Harmon, D.L.2    Nunez, F.3    Whitehead, A.S.4
  • 30
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spertroscopy
    • Jeener, J., Meier, B.H., Bachmann, P. & Ernst, R.R. Investigation of exchange processes by two-dimensional NMR spertroscopy. J. Chem. Phys. 71, 4546-4553 (1979).
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 31
    • 0344448273 scopus 로고
    • Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy
    • Braunschweiler, L. & Ernst, R.R. Coherence transfer by isotropic mixing: application to proton correlation spectroscopy. J. Magn. Reson. 53, 521-528 (1983).
    • (1983) J. Magn. Reson. , vol.53 , pp. 521-528
    • Braunschweiler, L.1    Ernst, R.R.2
  • 32
    • 33845378943 scopus 로고
    • Assignment of complex 1H NMR spectra via two-dimensional homonuclear Hartmann-Hahn spectroscopy
    • Davis, D.G. & Bax, A. Assignment of complex 1H NMR spectra via two-dimensional homonuclear Hartmann-Hahn spectroscopy. J. Am. Chem. Soc. 107, 2820-2821 (1985)
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 2820-2821
    • Davis, D.G.1    Bax, A.2
  • 33
    • 84946333474 scopus 로고
    • Analysis of networks of coupled spins by multiple quantum NMR
    • Braunschweiler, L., Bodenhause, G. & Ernst, R. R. Analysis of networks of coupled spins by multiple quantum NMR. Mol. Phys. 48, 535-560 (1983).
    • (1983) Mol. Phys. , vol.48 , pp. 535-560
    • Braunschweiler, L.1    Bodenhause, G.2    Ernst, R.R.3
  • 34
    • 0000195671 scopus 로고
    • Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy
    • Bodenhausen, G. & Ruben, D.J. Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy. Chem. Phys. Lett. 69, 185-200 (1980).
    • (1980) Chem. Phys. Lett. , vol.69 , pp. 185-200
    • Bodenhausen, G.1    Ruben, D.J.2
  • 35
    • 0000470905 scopus 로고
    • Heteronuclear three-dimensional NMR spectroscopy. a strategy for the simplification of homonuclear two-dimensional NMR spectra
    • Fesik, S.W. & Zuiderweg, E.R.P. Heteronuclear three-dimensional NMR spectroscopy. a strategy for the simplification of homonuclear two-dimensional NMR spectra. J. Magn. Reson. 78, 588-593 (1988).
    • (1988) J. Magn. Reson. , vol.78 , pp. 588-593
    • Fesik, S.W.1    Zuiderweg, E.R.P.2
  • 36
  • 37
    • 0024362326 scopus 로고
    • Overcoming the overlap problem in the assignment of 1H NMR spectra of larger proteins by use of three-dimensional heteronuclear 1H-15N Hartmann-Hahn-multiple quantum coherence and nuclear overhauser-multiple quantum coherence spectroscopy: Application to interleukin 1b
    • Marion, D. et al. Overcoming the overlap problem in the assignment of 1H NMR spectra of larger proteins by use of three-dimensional heteronuclear 1H-15N Hartmann-Hahn-multiple quantum coherence and nuclear overhauser-multiple quantum coherence spectroscopy: application to interleukin 1b. Biochemistry 28, 6150-6156 (1989).
    • (1989) Biochemistry , vol.28 , pp. 6150-6156
    • Marion, D.1
  • 38
    • 0025341339 scopus 로고
    • 15N spectra of larger proteins: Heteronuclear triple-resonance three-dimensional NMR spectroscopy. application to calmodulin
    • 15N spectra of larger proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. application to calmodulin. Biochemistry 29, 4659-4667 (1990).
    • (1990) Biochemistry , vol.29 , pp. 4659-4667
    • Ikura, M.1    Kay, L.E.2    Bax, A.3
  • 39
    • 44949291986 scopus 로고
    • Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins
    • Kay, L.E., Ikura, M., Tschudin, R. & Bax, A. Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins. J. Magn. Reson. 89, 496-514 (1990).
    • (1990) J. Magn. Reson. , vol.89 , pp. 496-514
    • Kay, L.E.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 40
    • 0026158667 scopus 로고
    • 15N backbone amide resonances with the a-carbon of the preceeding residue in uniformly 15N/13C enriched proteins
    • 15N backbone amide resonances with the a-carbon of the preceeding residue in uniformly 15N/13C enriched proteins. J. Biomol. NMR 1, 99-104 (1991).
    • (1991) J. Biomol. NMR , vol.1 , pp. 99-104
    • Bax, A.1    Ikura, M.2
  • 41
    • 0025374145 scopus 로고
    • Proton-proton correlation via carbon-carbon couplings: A three-dimensional NMR approach for the assignment of aliphatic resonances in proteins labeled with carbon-13
    • Kay, L. E., Ikura, M. & Bax, A. Proton-proton correlation via carbon-carbon couplings: a three-dimensional NMR approach for the assignment of aliphatic resonances in proteins labeled with carbon-13. J. Am. Chem. Soc. 112, 888-889 (1990).
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 888-889
    • Kay, L.E.1    Ikura, M.2    Bax, A.3
  • 43
    • 0025374145 scopus 로고
    • Proton-proton correlation via carbon-carbon couplings: A three-dimensional NMR approach for the assignment of aliphatic resonances in proteins labeled with carbon-13
    • Kay, L.E., Ikura, M. & Bax, A. Proton-proton correlation via carbon-carbon couplings: a three-dimensional NMR approach for the assignment of aliphatic resonances in proteins labeled with carbon-13. J. Am. Chem. Soc 112, 888-889 (1990)
    • (1990) J. Am. Chem. Soc , vol.112 , pp. 888-889
    • Kay, L.E.1    Ikura, M.2    Bax, A.3
  • 44
    • 0001210528 scopus 로고
    • FLATT - A new procedure for high-quality baseline correction of multidimensional NMR spectra
    • Güntert P. & Wüthrich, K. FLATT - a new procedure for high-quality baseline correction of multidimensional NMR spectra. J. Magn. Reson. 96, 403-407 (1992).
    • (1992) J. Magn. Reson. , vol.96 , pp. 403-407
    • Güntert, P.1    Wüthrich, K.2
  • 45
    • 45149137348 scopus 로고
    • New methods for the measurement of NH-CaH coupling constants in 15N-labeled proteins
    • Kay, L.E. & Bax, A. New methods for the measurement of NH-CaH coupling constants in 15N-labeled proteins. J. Magn. Reson. 86, 110-126 (1990).
    • (1990) J. Magn. Reson. , vol.86 , pp. 110-126
    • Kay, L.E.1    Bax, A.2
  • 46
    • 0024449503 scopus 로고
    • Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: Application to staphylococcal nuclease
    • Kay, L.E., Torchia, D.A. & Bax, A. Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease. Biochemistry 28, 8972-8979 (1989).
    • (1989) Biochemistry , vol.28 , pp. 8972-8979
    • Kay, L.E.1    Torchia, D.A.2    Bax, A.3
  • 48
    • 0026244229 scopus 로고
    • Molscript, a program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. Molscript, a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.