메뉴 건너뛰기




Volumn 61, Issue 1, 2007, Pages 61-67

The intrinsic flexibility of IgE and its role in binding FcεRI

Author keywords

CD; Fluorescence; Immunoglobulin E; Molten globule; NMR; Protein folding; Protein protein interactions

Indexed keywords

IMMUNOGLOBULIN E;

EID: 33846588989     PISSN: 07533322     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biopha.2006.11.004     Document Type: Article
Times cited : (12)

References (37)
  • 1
    • 0036883552 scopus 로고    scopus 로고
    • Molecular aspects of allergy
    • Miescher S.M., and Vogel M. Molecular aspects of allergy. Mol Aspects Med 23 (2002) 413-462
    • (2002) Mol Aspects Med , vol.23 , pp. 413-462
    • Miescher, S.M.1    Vogel, M.2
  • 2
    • 0034121188 scopus 로고    scopus 로고
    • Molecular genetics of allergic diseases
    • Ono S.J. Molecular genetics of allergic diseases. Annu Rev Immunol 18 (2000) 347-366
    • (2000) Annu Rev Immunol , vol.18 , pp. 347-366
    • Ono, S.J.1
  • 3
    • 0037134046 scopus 로고    scopus 로고
    • Allergy, parasites, and the hygiene hypothesis
    • Yazdanbakhsh M., Kremsner P.G., and van Ree R. Allergy, parasites, and the hygiene hypothesis. Science 296 (2002) 490-494
    • (2002) Science , vol.296 , pp. 490-494
    • Yazdanbakhsh, M.1    Kremsner, P.G.2    van Ree, R.3
  • 4
    • 33846608755 scopus 로고    scopus 로고
    • Drugs for the treatment of allergic disease
    • Holgate S.T., Church M.K., and Lichtenstein L.M. (Eds), Mosby International Ltd, London
    • Church M.K., and Makino S. Drugs for the treatment of allergic disease. In: Holgate S.T., Church M.K., and Lichtenstein L.M. (Eds). Allergy (2001), Mosby International Ltd, London
    • (2001) Allergy
    • Church, M.K.1    Makino, S.2
  • 5
    • 0033604544 scopus 로고    scopus 로고
    • The alliance of genes and environment in asthma and allergy
    • Cookson W. The alliance of genes and environment in asthma and allergy. Nature 402 (1999) B5-B11
    • (1999) Nature , vol.402
    • Cookson, W.1
  • 8
    • 0034948480 scopus 로고    scopus 로고
    • Monomeric IgE stimulates signaling pathways in mast cells that lead to cytokine production and cell survival
    • Kalesnikoff J., Huber M., Lam V., Damen J.E., Zhang J., Siraganian R.P., et al. Monomeric IgE stimulates signaling pathways in mast cells that lead to cytokine production and cell survival. Immunity 14 (2001) 801-811
    • (2001) Immunity , vol.14 , pp. 801-811
    • Kalesnikoff, J.1    Huber, M.2    Lam, V.3    Damen, J.E.4    Zhang, J.5    Siraganian, R.P.6
  • 9
    • 0036780841 scopus 로고    scopus 로고
    • Regulation of mast-cell and basophil function and survival by IgE
    • Kawakami T., and Galli S.J. Regulation of mast-cell and basophil function and survival by IgE. Nat Rev Immunol 2 (2002) 773-786
    • (2002) Nat Rev Immunol , vol.2 , pp. 773-786
    • Kawakami, T.1    Galli, S.J.2
  • 10
    • 0031443213 scopus 로고    scopus 로고
    • Participation of the N-terminal region of Cε3 in the binding of human IgE to its high-affinity receptor FcεRI
    • 15568-78
    • Henry A.J., Cook J.P., McDonnell J.M., Mackay G.A., Shi J., Sutton B.J., et al. Participation of the N-terminal region of Cε3 in the binding of human IgE to its high-affinity receptor FcεRI. Biochemistry 36 (1997) 15568-78
    • (1997) Biochemistry , vol.36
    • Henry, A.J.1    Cook, J.P.2    McDonnell, J.M.3    Mackay, G.A.4    Shi, J.5    Sutton, B.J.6
  • 11
    • 0034691520 scopus 로고    scopus 로고
    • Structure of the Fc fragment of human IgE bound to its high-affinity receptor FcεRIα
    • Garman S.C., Wurzburg B.A., Tarchevskaya S.S., Kinet J.P., and Jardetzky T.S. Structure of the Fc fragment of human IgE bound to its high-affinity receptor FcεRIα. Nature 406 (2000) 259-266
    • (2000) Nature , vol.406 , pp. 259-266
    • Garman, S.C.1    Wurzburg, B.A.2    Tarchevskaya, S.S.3    Kinet, J.P.4    Jardetzky, T.S.5
  • 12
    • 0028143496 scopus 로고
    • The binding site on human immunoglobulin E for its high affinity receptor
    • Presta L., Shields R., O'Connell L., Lahr S., Porter J., Gorman C., et al. The binding site on human immunoglobulin E for its high affinity receptor. J Biol Chem 269 (1994) 26368-26373
    • (1994) J Biol Chem , vol.269 , pp. 26368-26373
    • Presta, L.1    Shields, R.2    O'Connell, L.3    Lahr, S.4    Porter, J.5    Gorman, C.6
  • 13
    • 0029740925 scopus 로고    scopus 로고
    • A conformational rearrangement upon binding of IgE to its high affinity receptor
    • Sechi S., Roller P.P., Willette-Brown J., and Kinet J.P. A conformational rearrangement upon binding of IgE to its high affinity receptor. J Biol Chem 271 (1996) 19256-19263
    • (1996) J Biol Chem , vol.271 , pp. 19256-19263
    • Sechi, S.1    Roller, P.P.2    Willette-Brown, J.3    Kinet, J.P.4
  • 15
    • 0036308980 scopus 로고    scopus 로고
    • The crystal structure of IgE Fc reveals an asymmetrically bent conformation
    • Wan T., Beavil R.L., Fabiane S.M., Beavil A.J., Sohi M.K., Keown M., et al. The crystal structure of IgE Fc reveals an asymmetrically bent conformation. Nat Immunol 3 (2002) 681-686
    • (2002) Nat Immunol , vol.3 , pp. 681-686
    • Wan, T.1    Beavil, R.L.2    Fabiane, S.M.3    Beavil, A.J.4    Sohi, M.K.5    Keown, M.6
  • 16
    • 0036222835 scopus 로고    scopus 로고
    • Structural insights into the interactions between human IgE and its high affinity receptor FcεRI
    • Wurzburg B.A., and Jardetzky T.S. Structural insights into the interactions between human IgE and its high affinity receptor FcεRI. Mol Immunol 38 (2002) 1063-1072
    • (2002) Mol Immunol , vol.38 , pp. 1063-1072
    • Wurzburg, B.A.1    Jardetzky, T.S.2
  • 17
    • 0032587588 scopus 로고    scopus 로고
    • The immunoglobulin-like modules Cε3 and α2 are the minimal units necessary for human IgE-FcεRI interaction
    • Vangelista L., Laffer S., Turek R., Gronlund H., Sperr W.R., Valent P., et al. The immunoglobulin-like modules Cε3 and α2 are the minimal units necessary for human IgE-FcεRI interaction. J Clin Invest 103 (1999) 1571-1578
    • (1999) J Clin Invest , vol.103 , pp. 1571-1578
    • Vangelista, L.1    Laffer, S.2    Turek, R.3    Gronlund, H.4    Sperr, W.R.5    Valent, P.6
  • 18
    • 0034720689 scopus 로고    scopus 로고
    • Conformation of the isolated Cε3 domain of IgE and its complex with the high-affinity receptor, FcεRI
    • Henry A.J., McDonnell J.M., Ghirlando R., Sutton B.J., and Gould H.J. Conformation of the isolated Cε3 domain of IgE and its complex with the high-affinity receptor, FcεRI. Biochemistry 39 (2000) 7406-7413
    • (2000) Biochemistry , vol.39 , pp. 7406-7413
    • Henry, A.J.1    McDonnell, J.M.2    Ghirlando, R.3    Sutton, B.J.4    Gould, H.J.5
  • 20
    • 12544252739 scopus 로고    scopus 로고
    • The key role of protein flexibility in modulating IgE interactions
    • Price N.E., Price N.C., Kelly S.M., and McDonnell J.M. The key role of protein flexibility in modulating IgE interactions. J Biol Chem 280 (2005) 2324-2330
    • (2005) J Biol Chem , vol.280 , pp. 2324-2330
    • Price, N.E.1    Price, N.C.2    Kelly, S.M.3    McDonnell, J.M.4
  • 21
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn O.B. Molten globule and protein folding. Adv Protein Chem 47 (1995) 83-229
    • (1995) Adv Protein Chem , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 22
    • 0034744342 scopus 로고    scopus 로고
    • The structure of the IgE Cε2 domain and its role in stabilizing the complex with its high-affinity receptor FcεRIα
    • McDonnell J.M., Calvert R., Beavil R.L., Beavil A.J., Henry A.J., Sutton B.J., et al. The structure of the IgE Cε2 domain and its role in stabilizing the complex with its high-affinity receptor FcεRIα. Nat Struct Biol 8 (2001) 437-441
    • (2001) Nat Struct Biol , vol.8 , pp. 437-441
    • McDonnell, J.M.1    Calvert, R.2    Beavil, R.L.3    Beavil, A.J.4    Henry, A.J.5    Sutton, B.J.6
  • 23
    • 0033673325 scopus 로고    scopus 로고
    • Structure of the human IgE-Fc Cε3-Cε4 reveals conformational flexibility in the antibody effector domains
    • Wurzburg B.A., Garman S.C., and Jardetzky T.S. Structure of the human IgE-Fc Cε3-Cε4 reveals conformational flexibility in the antibody effector domains. Immunity 13 (2000) 375-385
    • (2000) Immunity , vol.13 , pp. 375-385
    • Wurzburg, B.A.1    Garman, S.C.2    Jardetzky, T.S.3
  • 24
    • 33645221313 scopus 로고    scopus 로고
    • Catalytic folding of the Cε3 domain by its high affinity receptor
    • Harwood N.E., Price N.C., and McDonnell J.M. Catalytic folding of the Cε3 domain by its high affinity receptor. FEBS Lett 580 (2006) 2129-2134
    • (2006) FEBS Lett , vol.580 , pp. 2129-2134
    • Harwood, N.E.1    Price, N.C.2    McDonnell, J.M.3
  • 26
  • 28
    • 0033642945 scopus 로고    scopus 로고
    • Structural stability of binding sites: consequences for binding affinity and allosteric effects
    • Luque I., and Freire E. Structural stability of binding sites: consequences for binding affinity and allosteric effects. Proteins 41 (2000) 63-71
    • (2000) Proteins , vol.41 , pp. 63-71
    • Luque, I.1    Freire, E.2
  • 29
    • 0015751224 scopus 로고
    • Thermally induced structural changes in immunoglobulin E
    • Dorrington K.J., and Bennich H. Thermally induced structural changes in immunoglobulin E. J Biol Chem 248 (1973) 8378-8384
    • (1973) J Biol Chem , vol.248 , pp. 8378-8384
    • Dorrington, K.J.1    Bennich, H.2
  • 30
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson H.J., and Wright P.E. Coupling of folding and binding for unstructured proteins. Curr Opin Struct Biol 12 (2002) 54-60
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 32
    • 0027443871 scopus 로고
    • Individual subunits of bacterial luciferase are molten globules and interact with molecular chaperones
    • Flynn G.C., Beckers C.J., Baase W.A., and Dahlquist F.W. Individual subunits of bacterial luciferase are molten globules and interact with molecular chaperones. Proc Natl Acad Sci U S A 90 (1993) 10826-10830
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 10826-10830
    • Flynn, G.C.1    Beckers, C.J.2    Baase, W.A.3    Dahlquist, F.W.4
  • 33
    • 0028067944 scopus 로고
    • The DNA recognition subunit of a DNA methyltransferase is predominantly a molten globule in the absence of DNA
    • Hornby D.P., Whitmarsh A., Pinarbasi H., Kelly S.M., Price N.C., Shore P., et al. The DNA recognition subunit of a DNA methyltransferase is predominantly a molten globule in the absence of DNA. FEBS Lett 355 (1994) 57-60
    • (1994) FEBS Lett , vol.355 , pp. 57-60
    • Hornby, D.P.1    Whitmarsh, A.2    Pinarbasi, H.3    Kelly, S.M.4    Price, N.C.5    Shore, P.6
  • 34
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson C.M. Protein folding and misfolding. Nature 426 (2003) 884-890
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 35
    • 0033200251 scopus 로고    scopus 로고
    • Folding studies of immunoglobulin-like β-sandwich proteins suggest that they share a common folding pathway
    • Clarke J., Cota E., Fowler S.B., and Hamill S.J. Folding studies of immunoglobulin-like β-sandwich proteins suggest that they share a common folding pathway. Structure Fold Des 7 (1999) 1145-1153
    • (1999) Structure Fold Des , vol.7 , pp. 1145-1153
    • Clarke, J.1    Cota, E.2    Fowler, S.B.3    Hamill, S.J.4
  • 37
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill K.A., and Chan H.S. From Levinthal to pathways to funnels. Nat Struct Biol 4 (1997) 10-19
    • (1997) Nat Struct Biol , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.