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Volumn 389, Issue 5, 2009, Pages 880-894

Contributions of Interfacial Residues of Human Interleukin15 to the Specificity and Affinity for Its Private α-Receptor

Author keywords

energetic hot spot; IL15; molecular recognition; protein protein interaction; surface plasmon resonance

Indexed keywords

INTERLEUKIN 15; INTERLEUKIN 15 RECEPTOR ALPHA;

EID: 67349282017     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.04.050     Document Type: Article
Times cited : (16)

References (54)
  • 2
    • 0035169507 scopus 로고    scopus 로고
    • Interleukin 15: biology and relevance to human disease
    • Fehniger T.A., and Caligiuri M.A. Interleukin 15: biology and relevance to human disease. Blood 97 (2001) 14-32
    • (2001) Blood , vol.97 , pp. 14-32
    • Fehniger, T.A.1    Caligiuri, M.A.2
  • 3
    • 0037073930 scopus 로고    scopus 로고
    • Maintenance of serological memory by polyclonal activation of human memory B cells
    • Bernasconi N.L., Traggiai E., and Lanzavecchia A. Maintenance of serological memory by polyclonal activation of human memory B cells. Science 298 (2002) 2199-2202
    • (2002) Science , vol.298 , pp. 2199-2202
    • Bernasconi, N.L.1    Traggiai, E.2    Lanzavecchia, A.3
  • 4
    • 33746547247 scopus 로고    scopus 로고
    • The biology of interleukin-2 and interleukin-15: implications for cancer therapy and vaccine design
    • Waldmann T.A. The biology of interleukin-2 and interleukin-15: implications for cancer therapy and vaccine design. Nat. Rev. Immunol. 6 (2006) 595-601
    • (2006) Nat. Rev. Immunol. , vol.6 , pp. 595-601
    • Waldmann, T.A.1
  • 5
    • 33645833872 scopus 로고    scopus 로고
    • The interleukin-15/interleukin-15 receptor system as a model for juxtacrine and reverse signaling
    • Bulfone-Paus S., Bulanova E., Budagian V., and Paus R. The interleukin-15/interleukin-15 receptor system as a model for juxtacrine and reverse signaling. Bioessays 28 (2006) 362-377
    • (2006) Bioessays , vol.28 , pp. 362-377
    • Bulfone-Paus, S.1    Bulanova, E.2    Budagian, V.3    Paus, R.4
  • 7
    • 0029099146 scopus 로고
    • Identification and cloning of a novel IL-15 binding protein that is structurally related to the α chain of the IL-2 receptor
    • Giri J.G., Kumaki S., Ahdieh M., Friend D.J., Loomis A., Shanebeck K., et al. Identification and cloning of a novel IL-15 binding protein that is structurally related to the α chain of the IL-2 receptor. EMBO J. 14 (1995) 3654-3663
    • (1995) EMBO J. , vol.14 , pp. 3654-3663
    • Giri, J.G.1    Kumaki, S.2    Ahdieh, M.3    Friend, D.J.4    Loomis, A.5    Shanebeck, K.6
  • 9
    • 34948886115 scopus 로고    scopus 로고
    • Targets of anticytokine therapy and the risk of infections in humans and mice
    • van de Vosse E., and van Agtmael M.A. Targets of anticytokine therapy and the risk of infections in humans and mice. Curr. Opin. Rheumatol. 19 (2007) 626-635
    • (2007) Curr. Opin. Rheumatol. , vol.19 , pp. 626-635
    • van de Vosse, E.1    van Agtmael, M.A.2
  • 10
    • 34247155347 scopus 로고    scopus 로고
    • Emerging cytokine targets in rheumatoid arthritis
    • Asquith D.L., and McInnes I.B. Emerging cytokine targets in rheumatoid arthritis. Curr. Opin. Rheumatol. 19 (2007) 246-251
    • (2007) Curr. Opin. Rheumatol. , vol.19 , pp. 246-251
    • Asquith, D.L.1    McInnes, I.B.2
  • 12
    • 0035399559 scopus 로고    scopus 로고
    • The Sushi domain of soluble IL-15 receptor α is essential for binding IL-15 and inhibiting inflammatory and allogenic responses in vitro and in vivo
    • Wei X.-Q., Orchardson M., Gracie J.A., Leung B.P., Bao-mei G., Guan H., et al. The Sushi domain of soluble IL-15 receptor α is essential for binding IL-15 and inhibiting inflammatory and allogenic responses in vitro and in vivo. J. Immunol. 167 (2001) 277-282
    • (2001) J. Immunol. , vol.167 , pp. 277-282
    • Wei, X.-Q.1    Orchardson, M.2    Gracie, J.A.3    Leung, B.P.4    Bao-mei, G.5    Guan, H.6
  • 13
    • 13344278015 scopus 로고
    • Functional characterization of the human interleukin-15 receptor alpha chain and close linkage of IL15RA and IL2RA genes
    • Anderson D.M., Kumaki S., Ahdieh M., Bertles J., Tometsko M., Loomis A., et al. Functional characterization of the human interleukin-15 receptor alpha chain and close linkage of IL15RA and IL2RA genes. J. Biol. Chem. 270 (1995) 29862-29869
    • (1995) J. Biol. Chem. , vol.270 , pp. 29862-29869
    • Anderson, D.M.1    Kumaki, S.2    Ahdieh, M.3    Bertles, J.4    Tometsko, M.5    Loomis, A.6
  • 14
    • 0141762622 scopus 로고    scopus 로고
    • On-column refolding and characterization of soluble human interleukin-15 receptor α-chain produced in Escherichia coli
    • Matsumoto M., Misawa S., Tsumoto K., Kumagai I., Hayashi H., and Kobayashi Y. On-column refolding and characterization of soluble human interleukin-15 receptor α-chain produced in Escherichia coli. Protein Expr. Purif. 31 (2003) 64-71
    • (2003) Protein Expr. Purif. , vol.31 , pp. 64-71
    • Matsumoto, M.1    Misawa, S.2    Tsumoto, K.3    Kumagai, I.4    Hayashi, H.5    Kobayashi, Y.6
  • 15
    • 33644975335 scopus 로고    scopus 로고
    • Soluble interleukin-15 receptor α (IL-15R α)-sushi as a selective and potent agonist of IL-15 action through IL-15R β/γ
    • Mortier E., Quéméner A., Vusio P., Lorenzen I., Boublik Y., Grötzinger J., et al. Soluble interleukin-15 receptor α (IL-15R α)-sushi as a selective and potent agonist of IL-15 action through IL-15R β/γ. J. Biol. Chem. 281 (2006) 1612-1619
    • (2006) J. Biol. Chem. , vol.281 , pp. 1612-1619
    • Mortier, E.1    Quéméner, A.2    Vusio, P.3    Lorenzen, I.4    Boublik, Y.5    Grötzinger, J.6
  • 16
    • 20344387872 scopus 로고    scopus 로고
    • The structure of interleukin-2 complexed with its alpha receptor
    • Rickert M., Wang X., Boulanger M., Goriatcheva N., and Garcia K.C. The structure of interleukin-2 complexed with its alpha receptor. Science 308 (2005) 1477-1480
    • (2005) Science , vol.308 , pp. 1477-1480
    • Rickert, M.1    Wang, X.2    Boulanger, M.3    Goriatcheva, N.4    Garcia, K.C.5
  • 18
    • 33750076967 scopus 로고    scopus 로고
    • Docking of human interleukin-15 to its specific receptor α chain: correlation between molecular modeling and mutagenesis experimental data
    • Quéméner A., Bernard J., Mortier E., Plet A., Jacques Y., and Tran V. Docking of human interleukin-15 to its specific receptor α chain: correlation between molecular modeling and mutagenesis experimental data. Proteins 65 (2006) 623-636
    • (2006) Proteins , vol.65 , pp. 623-636
    • Quéméner, A.1    Bernard, J.2    Mortier, E.3    Plet, A.4    Jacques, Y.5    Tran, V.6
  • 19
    • 0027764465 scopus 로고
    • Contribution of buried hydrogen bonds to protein stability. The crystal structures of two barnase mutants
    • Chen Y.W., Fersht A.R., and Henrick K. Contribution of buried hydrogen bonds to protein stability. The crystal structures of two barnase mutants. J. Mol. Biol. 234 (1993) 1158-1170
    • (1993) J. Mol. Biol. , vol.234 , pp. 1158-1170
    • Chen, Y.W.1    Fersht, A.R.2    Henrick, K.3
  • 20
    • 44349192157 scopus 로고    scopus 로고
    • Crystal structural analysis of protein-protein interactions drastically destabilized by a single mutation
    • Urakubo Y., Ikura T., and Ito N. Crystal structural analysis of protein-protein interactions drastically destabilized by a single mutation. Protein Sci. 17 (2008) 1055-1065
    • (2008) Protein Sci. , vol.17 , pp. 1055-1065
    • Urakubo, Y.1    Ikura, T.2    Ito, N.3
  • 21
    • 34548125264 scopus 로고    scopus 로고
    • Crystal structure of the IL-15-IL-15Rα complex, a cytokine-receptor unit presented in trans
    • Chirifu M., Hayashi C., Nakamura T., Toma S., Shuto T., Kai H., et al. Crystal structure of the IL-15-IL-15Rα complex, a cytokine-receptor unit presented in trans. Nat. Immunol. 8 (2007) 1001-1007
    • (2007) Nat. Immunol. , vol.8 , pp. 1001-1007
    • Chirifu, M.1    Hayashi, C.2    Nakamura, T.3    Toma, S.4    Shuto, T.5    Kai, H.6
  • 23
    • 34250315356 scopus 로고    scopus 로고
    • Structural consequences of mutations in interfacial Tyr residues of a protein antigen-antibody complex
    • Shiroishi M., Tsumoto K., Tanaka Y., Yokota A., Nakanishi T., Kondo H., and Kumagai I. Structural consequences of mutations in interfacial Tyr residues of a protein antigen-antibody complex. J. Biol. Chem. 282 (2007) 6783-6791
    • (2007) J. Biol. Chem. , vol.282 , pp. 6783-6791
    • Shiroishi, M.1    Tsumoto, K.2    Tanaka, Y.3    Yokota, A.4    Nakanishi, T.5    Kondo, H.6    Kumagai, I.7
  • 24
    • 0036708467 scopus 로고    scopus 로고
    • Relationship between ion pair geometries and electrostatic strengths in proteins
    • Kumar S., and Nussinov R. Relationship between ion pair geometries and electrostatic strengths in proteins. Biophys. J. 83 (2002) 1595-1612
    • (2002) Biophys. J. , vol.83 , pp. 1595-1612
    • Kumar, S.1    Nussinov, R.2
  • 25
    • 0036306236 scopus 로고    scopus 로고
    • On the role of electrostatic interactions in the design of protein-protein interfaces
    • Sheinerman F.B., and Honig B. On the role of electrostatic interactions in the design of protein-protein interfaces. J. Mol. Biol. 318 (2002) 161-177
    • (2002) J. Mol. Biol. , vol.318 , pp. 161-177
    • Sheinerman, F.B.1    Honig, B.2
  • 27
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • Clackson T., and Wells J.A. A hot spot of binding energy in a hormone-receptor interface. Science 267 (1995) 383-386
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 28
    • 0032479179 scopus 로고    scopus 로고
    • Anatomy of hot spots in protein interfaces
    • Bogan A.A., and Thorn K.S. Anatomy of hot spots in protein interfaces. J. Mol. Biol. 280 (1998) 1-9
    • (1998) J. Mol. Biol. , vol.280 , pp. 1-9
    • Bogan, A.A.1    Thorn, K.S.2
  • 29
    • 0036469060 scopus 로고    scopus 로고
    • Unraveling hot spots in binding interfaces: progress and challenges
    • DeLano W.L. Unraveling hot spots in binding interfaces: progress and challenges. Curr. Opin. Struct. Biol. 12 (2002) 14-20
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 14-20
    • DeLano, W.L.1
  • 30
    • 0037008160 scopus 로고    scopus 로고
    • Approaches to the description and prediction of the binding affinity of small-molecule ligands to macromolecular receptors
    • Gohlke H., and Klebe G. Approaches to the description and prediction of the binding affinity of small-molecule ligands to macromolecular receptors. Angew. Chem. Int. Ed. Engl. 41 (2002) 2644-2676
    • (2002) Angew. Chem. Int. Ed. Engl. , vol.41 , pp. 2644-2676
    • Gohlke, H.1    Klebe, G.2
  • 31
    • 48249102785 scopus 로고    scopus 로고
    • Calorimetry and thermodynamics in drug design
    • Chaires J.B. Calorimetry and thermodynamics in drug design. Annu. Rev. Biophys. 37 (2008) 135-151
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 135-151
    • Chaires, J.B.1
  • 32
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • Lo Conte L., Chothia C., and Janin J. The atomic structure of protein-protein recognition sites. J. Mol. Biol. 285 (1999) 2177-2198
    • (1999) J. Mol. Biol. , vol.285 , pp. 2177-2198
    • Lo Conte, L.1    Chothia, C.2    Janin, J.3
  • 33
    • 0036424666 scopus 로고    scopus 로고
    • Structural basis of macromolecular recognition
    • Wodak S.J., and Janin J. Structural basis of macromolecular recognition. Adv. Protein Chem. 61 (2002) 9-73
    • (2002) Adv. Protein Chem. , vol.61 , pp. 9-73
    • Wodak, S.J.1    Janin, J.2
  • 35
    • 0030582682 scopus 로고    scopus 로고
    • Dominant forces in the recognition of a transient folding intermediate of alpha-lactalbumin by GroEL
    • Katsumata K., Okazaki A., Tsurupa G.P., and Kuwajima K. Dominant forces in the recognition of a transient folding intermediate of alpha-lactalbumin by GroEL. J. Mol. Biol. 264 (1996) 643-649
    • (1996) J. Mol. Biol. , vol.264 , pp. 643-649
    • Katsumata, K.1    Okazaki, A.2    Tsurupa, G.P.3    Kuwajima, K.4
  • 36
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reactions: forces contributing to stability
    • Ross P.D., and Subramanian S. Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry 20 (1981) 3096-3102
    • (1981) Biochemistry , vol.20 , pp. 3096-3102
    • Ross, P.D.1    Subramanian, S.2
  • 37
    • 0032845707 scopus 로고    scopus 로고
    • Energetics of substrate binding, catalysis, and product release
    • Cleland W.W., and Northrop D.B. Energetics of substrate binding, catalysis, and product release. Methods Enzymol. 308 (1999) 3-27
    • (1999) Methods Enzymol. , vol.308 , pp. 3-27
    • Cleland, W.W.1    Northrop, D.B.2
  • 38
    • 40149098874 scopus 로고    scopus 로고
    • Entropy drives integrin αIIbβ3:echistatin binding-evidence from surface plasmon resonance spectroscopy
    • Hantgan R.R., Stahle M.C., and Horita D.A. Entropy drives integrin αIIbβ3:echistatin binding-evidence from surface plasmon resonance spectroscopy. Biochemistry 47 (2008) 2884-2892
    • (2008) Biochemistry , vol.47 , pp. 2884-2892
    • Hantgan, R.R.1    Stahle, M.C.2    Horita, D.A.3
  • 39
    • 37549007225 scopus 로고    scopus 로고
    • Crystal Structure of the interleukin-15·interleukin-15 receptor α complex: insights into trans and cis presentation
    • Olsen S.K., Ota N., Kishishita S., Kukimoto-Niino M., Murayama K., Uchiyama H., et al. Crystal Structure of the interleukin-15·interleukin-15 receptor α complex: insights into trans and cis presentation. J. Biol. Chem. 282 (2007) 37191-37204
    • (2007) J. Biol. Chem. , vol.282 , pp. 37191-37204
    • Olsen, S.K.1    Ota, N.2    Kishishita, S.3    Kukimoto-Niino, M.4    Murayama, K.5    Uchiyama, H.6
  • 40
    • 0029564595 scopus 로고
    • Are buried salt bridges important for protein stability and conformational specificity?
    • Waldburger C.D., Schildbach J.F., and Sauer R.T. Are buried salt bridges important for protein stability and conformational specificity?. Nat. Struct. Biol. 2 (1995) 122-128
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 122-128
    • Waldburger, C.D.1    Schildbach, J.F.2    Sauer, R.T.3
  • 41
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E., and Henrick K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372 (2007) 774-797
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 42
  • 43
    • 0026567907 scopus 로고
    • Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect
    • Eriksson A.E., Baase W.A., Zhang X.J., Heinz D.W., Blaber M., Baldwin E.P., and Matthews B.W. Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect. Science 255 (1995) 178-183
    • (1995) Science , vol.255 , pp. 178-183
    • Eriksson, A.E.1    Baase, W.A.2    Zhang, X.J.3    Heinz, D.W.4    Blaber, M.5    Baldwin, E.P.6    Matthews, B.W.7
  • 44
    • 0029882171 scopus 로고    scopus 로고
    • Structural and energetic responses to cavity-creating mutations in hydrophobic cores: observation of a buried water molecule and the hydrophilic nature of such hydrophobic cavities
    • Buckle A.M., Cramer P., and Fersht A.R. Structural and energetic responses to cavity-creating mutations in hydrophobic cores: observation of a buried water molecule and the hydrophilic nature of such hydrophobic cavities. Biochemistry 35 (1996) 4298-4305
    • (1996) Biochemistry , vol.35 , pp. 4298-4305
    • Buckle, A.M.1    Cramer, P.2    Fersht, A.R.3
  • 45
    • 0034633945 scopus 로고    scopus 로고
    • Thermodynamic and structural studies of cavity formation in proteins suggest that loss of packing interactions rather than the hydrophobic effect dominates the observed energetics
    • Ratnaparkhi G.S., and Varadarajan R. Thermodynamic and structural studies of cavity formation in proteins suggest that loss of packing interactions rather than the hydrophobic effect dominates the observed energetics. Biochemistry 39 (2000) 12365-12374
    • (2000) Biochemistry , vol.39 , pp. 12365-12374
    • Ratnaparkhi, G.S.1    Varadarajan, R.2
  • 46
    • 49549098143 scopus 로고    scopus 로고
    • The exon-3-encoded domain of IL-15Rα contributes to IL-15 high-affinity binding and is crucial for the IL-15 antagonistic effect of soluble IL-15Rα
    • Bouchaud G., Garrigue-Antar L., Solé V., Quéméner A., Boublik Y., Mortier E., et al. The exon-3-encoded domain of IL-15Rα contributes to IL-15 high-affinity binding and is crucial for the IL-15 antagonistic effect of soluble IL-15Rα. J. Mol. Biol. 382 (2008) 1-12
    • (2008) J. Mol. Biol. , vol.382 , pp. 1-12
    • Bouchaud, G.1    Garrigue-Antar, L.2    Solé, V.3    Quéméner, A.4    Boublik, Y.5    Mortier, E.6
  • 47
    • 0027772959 scopus 로고
    • Shape complementarity at protein/protein interfaces
    • Lawrence M.C., and Colman P.M. Shape complementarity at protein/protein interfaces. J. Mol. Biol. 234 (1993) 946-950
    • (1993) J. Mol. Biol. , vol.234 , pp. 946-950
    • Lawrence, M.C.1    Colman, P.M.2
  • 48
    • 0038813750 scopus 로고    scopus 로고
    • The role of hydrogen bonding via interfacial water molecules in antigen-antibody complexation
    • Yokota A., Tsumoto K., Shiroishi M., Kondo H., and Kumagai I. The role of hydrogen bonding via interfacial water molecules in antigen-antibody complexation. J. Biol. Chem. 278 (2003) 5410-5418
    • (2003) J. Biol. Chem. , vol.278 , pp. 5410-5418
    • Yokota, A.1    Tsumoto, K.2    Shiroishi, M.3    Kondo, H.4    Kumagai, I.5
  • 49
    • 0028276796 scopus 로고
    • A lymphokine, provisionally designated interleukin T and produced by a human adult T-cell leukemia line, stimulates T-cell proliferation and the induction of lymphokine-activated killer cells
    • Burton J.D., Bamford R.N., Peters C., Grant A.J., Kurys G., Goldman C.K., et al. A lymphokine, provisionally designated interleukin T and produced by a human adult T-cell leukemia line, stimulates T-cell proliferation and the induction of lymphokine-activated killer cells. Proc. Natl Acad. Sci. USA 91 (1994) 4935-4939
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 4935-4939
    • Burton, J.D.1    Bamford, R.N.2    Peters, C.3    Grant, A.J.4    Kurys, G.5    Goldman, C.K.6
  • 50
    • 0028179054 scopus 로고
    • Cloning of a T cell growth factor that interacts with the β chain of the interleukin-2 receptor
    • Grabstein K.H., Eisenman J., Shanebeck K., Rauch C., Srinivasan S., Fung V., et al. Cloning of a T cell growth factor that interacts with the β chain of the interleukin-2 receptor. Science 264 (1994) 965-968
    • (1994) Science , vol.264 , pp. 965-968
    • Grabstein, K.H.1    Eisenman, J.2    Shanebeck, K.3    Rauch, C.4    Srinivasan, S.5    Fung, V.6
  • 52
    • 33750303565 scopus 로고    scopus 로고
    • Hot-spot mimicry of a cytokine receptor by a small molecule
    • Thanos C.D., DeLano W.L., and Wells J.A. Hot-spot mimicry of a cytokine receptor by a small molecule. Proc. Natl Acad. Sci. USA 103 (2006) 15422-15427
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 15422-15427
    • Thanos, C.D.1    DeLano, W.L.2    Wells, J.A.3
  • 53
    • 0032191701 scopus 로고    scopus 로고
    • Highly efficient recovery of functional single-chain Fv fragments from inclusion bodies overexpressed in Escherichia coli by controlled introduction of oxidizing reagent-application to a human single-chain Fv fragment
    • Tsumoto K., Shinoki K., Kondo H., Uchikawa M., Juji T., and Kumagai I. Highly efficient recovery of functional single-chain Fv fragments from inclusion bodies overexpressed in Escherichia coli by controlled introduction of oxidizing reagent-application to a human single-chain Fv fragment. J. Immunol. Methods 219 (1998) 119-129
    • (1998) J. Immunol. Methods , vol.219 , pp. 119-129
    • Tsumoto, K.1    Shinoki, K.2    Kondo, H.3    Uchikawa, M.4    Juji, T.5    Kumagai, I.6
  • 54
    • 0037174127 scopus 로고    scopus 로고
    • Antitumor activity of interleukin-21 prepared by novel refolding procedure from inclusion bodies expressed in Escherichia coli
    • Asano R., Kudo T., Makabe K., Tsumoto K., and Kumagai I. Antitumor activity of interleukin-21 prepared by novel refolding procedure from inclusion bodies expressed in Escherichia coli. FEBS Lett. 528 (2002) 70-76
    • (2002) FEBS Lett. , vol.528 , pp. 70-76
    • Asano, R.1    Kudo, T.2    Makabe, K.3    Tsumoto, K.4    Kumagai, I.5


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