메뉴 건너뛰기




Volumn 44, Issue 33, 2005, Pages 11106-11114

IL-1β epitope mapping using site-directed mutagenesis and hydrogen-deuterium exchange mass spectrometry analysis

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CONCENTRATION (PROCESS); CRYSTAL STRUCTURE; HYDROPHOBICITY; MASS SPECTROMETRY; MUTAGENESIS; SURFACE PLASMON RESONANCE;

EID: 23944523304     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0505464     Document Type: Article
Times cited : (29)

References (37)
  • 1
    • 0031801957 scopus 로고    scopus 로고
    • Signal transduction pathways activated by the IL-1 receptor family: Ancient signaling machinery in mammals, insects, and plants
    • O'Neill, L. A., and Greene, C. (1998) Signal transduction pathways activated by the IL-1 receptor family: Ancient signaling machinery in mammals, insects, and plants, J. Leukocyte Biol. 63, 650-657.
    • (1998) J. Leukocyte Biol. , vol.63 , pp. 650-657
    • O'Neill, L.A.1    Greene, C.2
  • 2
    • 0344196965 scopus 로고    scopus 로고
    • The Interleukin 1 (IL-1) receptor: Ligand interactions and signal transduction
    • Auron, P. E. (1998) The Interleukin 1 (IL-1) receptor: Ligand interactions and signal transduction, Cytokine Growth Factor Rev. 9, 221-237.
    • (1998) Cytokine Growth Factor Rev. , vol.9 , pp. 221-237
    • Auron, P.E.1
  • 3
    • 0028233509 scopus 로고
    • The two interleukin-1 receptors play different roles in IL-1 actions
    • Sims, J. E., Giri, J. G., and Dower, S. K. (1994) The two interleukin-1 receptors play different roles in IL-1 actions, Clin. Immunol. Immunopathol. 72, 9-14.
    • (1994) Clin. Immunol. Immunopathol. , vol.72 , pp. 9-14
    • Sims, J.E.1    Giri, J.G.2    Dower, S.K.3
  • 4
    • 0034657781 scopus 로고    scopus 로고
    • IL-1 signaling cascade in liver cells and the involvement of a soluble form of the IL-1 receptor accessory protein
    • Jensen, L. E., Muzio, M., Mantovani, A., and Whitehead, A. S. (2000) IL-1 signaling cascade in liver cells and the involvement of a soluble form of the IL-1 receptor accessory protein, J. Immunol. 164, 5277-5286.
    • (2000) J. Immunol. , vol.164 , pp. 5277-5286
    • Jensen, L.E.1    Muzio, M.2    Mantovani, A.3    Whitehead, A.S.4
  • 5
    • 0032534729 scopus 로고    scopus 로고
    • The type II IL-1 receptor interacts with the IL-1 receptor accessory protein: A novel mechanism of regulation of IL-1 responsiveness
    • Lang, D., Knop, J., Wesche, H., Raffetseder, U., Kurrle, R., Boraschi, D., and Martin, M. U. (1998) The type II IL-1 receptor interacts with the IL-1 receptor accessory protein: A novel mechanism of regulation of IL-1 responsiveness, J. Immunol. 161, 6871-6877.
    • (1998) J. Immunol. , vol.161 , pp. 6871-6877
    • Lang, D.1    Knop, J.2    Wesche, H.3    Raffetseder, U.4    Kurrle, R.5    Boraschi, D.6    Martin, M.U.7
  • 6
    • 0028004236 scopus 로고
    • The type II "decoy" receptor: A novel regulatory pathway for interleukin 1
    • Colotta, F., Dower, S. K., Sims, J. E., and Mantovani, A. (1994) The type II "decoy" receptor: A novel regulatory pathway for interleukin 1, Immunol. Today 15, 562-566.
    • (1994) Immunol. Today , vol.15 , pp. 562-566
    • Colotta, F.1    Dower, S.K.2    Sims, J.E.3    Mantovani, A.4
  • 8
    • 0028172557 scopus 로고
    • Binding of IL-1α, IL-1β, and IL-1 receptor antagonist by soluble IL-1 receptors and levels of soluble IL-1 receptors in synovial fluids
    • Arend, W. P., Malyak, M., Smith, M. F., Jr., Whisenand, T. D., Slack, J. L., Sims, J. E., Giri, J. G., and Dower, S. K. (1994) Binding of IL-1α, IL-1β, and IL-1 receptor antagonist by soluble IL-1 receptors and levels of soluble IL-1 receptors in synovial fluids, J. Immunol. 153, 4766-4774.
    • (1994) J. Immunol. , vol.153 , pp. 4766-4774
    • Arend, W.P.1    Malyak, M.2    Smith Jr., M.F.3    Whisenand, T.D.4    Slack, J.L.5    Sims, J.E.6    Giri, J.G.7    Dower, S.K.8
  • 10
    • 0036400340 scopus 로고    scopus 로고
    • Anakinra as a new therapeutic option in rheumatoid arthritis: Clinical results and perspectives
    • Bresnihan, B. (2002) Anakinra as a new therapeutic option in rheumatoid arthritis: Clinical results and perspectives, Clin. Exp. Rheumatol. 20, S32-S34.
    • (2002) Clin. Exp. Rheumatol. , vol.20
    • Bresnihan, B.1
  • 11
    • 9144261181 scopus 로고    scopus 로고
    • Single and combined inhibition of tumor necrosis factor, interleukin-1, and RANKL pathways in tumor necrosis factor-induced arthritis: Effects on synovial inflammation, bone erosion, and cartilage destruction
    • Zwerina, J., Hayer, S., Tohidast-Akrad, M., Bergmeister, H., Redlich, K., Feige, U., Dunstan, C., Kollias, G., Steiner, G., Smolen, J., and Schett, G. (2004) Single and combined inhibition of tumor necrosis factor, interleukin-1, and RANKL pathways in tumor necrosis factor-induced arthritis: Effects on synovial inflammation, bone erosion, and cartilage destruction, Arthritis Rheum. 50, 277-290.
    • (2004) Arthritis Rheum. , vol.50 , pp. 277-290
    • Zwerina, J.1    Hayer, S.2    Tohidast-Akrad, M.3    Bergmeister, H.4    Redlich, K.5    Feige, U.6    Dunstan, C.7    Kollias, G.8    Steiner, G.9    Smolen, J.10    Schett, G.11
  • 13
    • 0023957427 scopus 로고
    • Crystal structure of the cytokine interleukin-1β
    • Priestle, J. P., Schar, H. P., and Grutter, M. G. (1988) Crystal structure of the cytokine interleukin-1β, EMBO J. 7, 339-343.
    • (1988) EMBO J. , vol.7 , pp. 339-343
    • Priestle, J.P.1    Schar, H.P.2    Grutter, M.G.3
  • 18
    • 0037058888 scopus 로고    scopus 로고
    • Glycosylation of erythropoietin affects receptor binding kinetics: Role of electrostatic interactions
    • Darling, R. J., Kuchibhotla, U., Glaesner, W., Micanovic, R., Witcher, D. R., and Beals, J. M. (2002) Glycosylation of erythropoietin affects receptor binding kinetics: Role of electrostatic interactions, Biochemistry 41, 14524-14531.
    • (2002) Biochemistry , vol.41 , pp. 14524-14531
    • Darling, R.J.1    Kuchibhotla, U.2    Glaesner, W.3    Micanovic, R.4    Witcher, D.R.5    Beals, J.M.6
  • 19
    • 0027053116 scopus 로고
    • Electrostatic interactions in the association of proteins: An analysis of the thrombin-hirudin complex
    • Karshikov, A., Bode, W., Tulinsky, A., and Stone, S. R. (1992) Electrostatic interactions in the association of proteins: An analysis of the thrombin-hirudin complex, Protein Sci. 1, 727-735.
    • (1992) Protein Sci. , vol.1 , pp. 727-735
    • Karshikov, A.1    Bode, W.2    Tulinsky, A.3    Stone, S.R.4
  • 20
    • 0033605858 scopus 로고    scopus 로고
    • Predicting the rate enhancement of protein complex formation from the electrostatic energy of interaction
    • Selzer, T., and Schreiber, G. (1999) Predicting the rate enhancement of protein complex formation from the electrostatic energy of interaction, J. Mol. Biol. 287, 409-419.
    • (1999) J. Mol. Biol. , vol.287 , pp. 409-419
    • Selzer, T.1    Schreiber, G.2
  • 21
    • 0033923367 scopus 로고    scopus 로고
    • Rational design of faster associating and tighter binding protein complexes
    • Selzer, T., Albeck, S., and Schreiber, G. (2000) Rational design of faster associating and tighter binding protein complexes, Nat. Struct. Biol. 7, 537-541.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 537-541
    • Selzer, T.1    Albeck, S.2    Schreiber, G.3
  • 22
    • 0035889692 scopus 로고    scopus 로고
    • New insights into the mechanism of protein-protein association
    • Selzer, T., and Schreiber, G. (2001) New insights into the mechanism of protein-protein association, Proteins 45, 190-198.
    • (2001) Proteins , vol.45 , pp. 190-198
    • Selzer, T.1    Schreiber, G.2
  • 23
    • 0031012271 scopus 로고    scopus 로고
    • Very rapid, ionic strength-dependent association and folding of a heterodimeric leucine zipper
    • Wendt, H., Leder, L., Harma, H., Jelesarov, I., Baici, A., and Bosshard, H. R. (1997) Very rapid, ionic strength-dependent association and folding of a heterodimeric leucine zipper. Biochemistry 36, 204-213.
    • (1997) Biochemistry , vol.36 , pp. 204-213
    • Wendt, H.1    Leder, L.2    Harma, H.3    Jelesarov, I.4    Baici, A.5    Bosshard, H.R.6
  • 24
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. A., and Honig, B. (1991) Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons, Proteins 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 25
    • 0029046142 scopus 로고
    • Mapping receptor binding sites in interleukin (IL)-1 receptor antagonist and IL-1β by site-directed mutagenesis. Identification of a single site in IL-1ra and two sites in IL-1β
    • Evans, R. J., Bray, J., Childs, J. D., Vigers, G. P., Brandhuber, B. J., Skalicky, J. J., Thompson, R. C., and Eisenberg, S. P. (1995) Mapping receptor binding sites in interleukin (IL)-1 receptor antagonist and IL-1β by site-directed mutagenesis. Identification of a single site in IL-1ra and two sites in IL-1β, J. Biol. Chem. 270, 11477-11483.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11477-11483
    • Evans, R.J.1    Bray, J.2    Childs, J.D.3    Vigers, G.P.4    Brandhuber, B.J.5    Skalicky, J.J.6    Thompson, R.C.7    Eisenberg, S.P.8
  • 26
    • 0028354297 scopus 로고
    • A mutational analysis of receptor binding sites of interleukin-1β: Differences in binding of human interleukin-1β muteins to human and mouse receptors
    • Grutter, M. G., van Oostrum, J., Priestle, J. P., Edelmann, E., Joss, U., Feige, U., Vosbeck, K., and Schmitz, A. (1994) A mutational analysis of receptor binding sites of interleukin-1β: Differences in binding of human interleukin-1β muteins to human and mouse receptors, Protein Eng. 7, 663-671.
    • (1994) Protein Eng. , vol.7 , pp. 663-671
    • Grutter, M.G.1    Van Oostrum, J.2    Priestle, J.P.3    Edelmann, E.4    Joss, U.5    Feige, U.6    Vosbeck, K.7    Schmitz, A.8
  • 28
    • 0030998098 scopus 로고    scopus 로고
    • Crystal siruclure of the type-I interleukin-1 receptor complexed with interleukin-1β
    • Vigers, G. P., Anderson, L. J., Caffes, P., and Brandhuber, B. J. (1997) Crystal siruclure of the type-I interleukin-1 receptor complexed with interleukin-1β, Nature 386, 190-194.
    • (1997) Nature , vol.386 , pp. 190-194
    • Vigers, G.P.1    Anderson, L.J.2    Caffes, P.3    Brandhuber, B.J.4
  • 30
    • 1842863972 scopus 로고    scopus 로고
    • Practical methods for deuterium exchange/mass spectrometry
    • Hoofnagle, A. N., Resing, K. A., and Ahn, N. G. (2004) Practical methods for deuterium exchange/mass spectrometry. Methods Mol. Biol. 250, 283-298.
    • (2004) Methods Mol. Biol. , vol.250 , pp. 283-298
    • Hoofnagle, A.N.1    Resing, K.A.2    Ahn, N.G.3
  • 32
    • 0036102156 scopus 로고    scopus 로고
    • Epitope mapping of a monoclonal antibody against human thrombin by H/D-exchange mass spectrometry reveals selection of a diverse sequence in a highly conserved protein
    • Baerga-Ortiz, A., Hughes, C. A., Mandell, J. G., and Komives, E. A. (2002) Epitope mapping of a monoclonal antibody against human thrombin by H/D-exchange mass spectrometry reveals selection of a diverse sequence in a highly conserved protein, Protein Sci. 11, 1300-1308.
    • (2002) Protein Sci. , vol.11 , pp. 1300-1308
    • Baerga-Ortiz, A.1    Hughes, C.A.2    Mandell, J.G.3    Komives, E.A.4
  • 33
    • 0033557450 scopus 로고    scopus 로고
    • Hydrogen exchange/electrospray ionization mass spectrometry studies of structural features of proteins and protein/ protein interactions
    • Ehring, H. (1999) Hydrogen exchange/electrospray ionization mass spectrometry studies of structural features of proteins and protein/ protein interactions, Anal. Biochem. 267, 252-259.
    • (1999) Anal. Biochem. , vol.267 , pp. 252-259
    • Ehring, H.1
  • 35
    • 0035753065 scopus 로고    scopus 로고
    • High resolution, high-throughput amide deuterium exchange-mass spectrometry (DXMS) determination of protein binding site structure and dynamics: Utility in pharmaceutical design
    • Woods, V. L., Jr., and Hamuro, Y. (2001) High resolution, high-throughput amide deuterium exchange-mass spectrometry (DXMS) determination of protein binding site structure and dynamics: Utility in pharmaceutical design, J. Cell. Biochem. Suppl. 89-98.
    • (2001) J. Cell. Biochem. Suppl. , pp. 89-98
    • Woods Jr., V.L.1    Hamuro, Y.2
  • 36
    • 1442333529 scopus 로고    scopus 로고
    • Modeling data from titration, amide H/D exchange, and mass spectrometry to obtain protein-ligand binding constants
    • Zhu, M. M., Rempel, D. L., and Gross, M. L. (2004) Modeling data from titration, amide H/D exchange, and mass spectrometry to obtain protein-ligand binding constants, J. Am. Soc. Mass Spectrom. 15, 388-397.
    • (2004) J. Am. Soc. Mass Spectrom. , vol.15 , pp. 388-397
    • Zhu, M.M.1    Rempel, D.L.2    Gross, M.L.3
  • 37
    • 0033655078 scopus 로고    scopus 로고
    • Investigating the higher order structure of proteins. Hydrogen exchange, proteolytic fragmentation, and mass spectrometry
    • Engen, J. R., and Smith, D. L. (2000) Investigating the higher order structure of proteins. Hydrogen exchange, proteolytic fragmentation, and mass spectrometry, Methods Mol. Biol. 146, 95-112.
    • (2000) Methods Mol. Biol. , vol.146 , pp. 95-112
    • Engen, J.R.1    Smith, D.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.