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Garman, S. C., Wurzburg, B. A., Tarchevskaya, S. S., Kinet, J.-P., & Jardetzky, T. S. (2000). Structure of the Fc fragment of human IgE bound to its high-affinity receptor FcεRIα. Nature, 406(6793), 259–266.

Authors 5
  1. Scott C. Garman (first)
  2. Beth A. Wurzburg (additional)
  3. Svetlana S. Tarchevskaya (additional)
  4. Jean-Pierre Kinet (additional)
  5. Theodore S. Jardetzky (additional)
References 50 Referenced 299
  1. Metzger, H. The receptor with high affinity for IgE. Immunol. Rev. 125, 37–48 (1992). (10.1111/j.1600-065X.1992.tb00624.x) / Immunol. Rev. by H Metzger (1992)
  2. Kinet, J. P. The high-affinity IgE receptor (FcεRI): from physiology to pathology. Annu. Rev. Immunol. 17, 931– 972 (1999). (10.1146/annurev.immunol.17.1.931) / Annu. Rev. Immunol. by JP Kinet (1999)
  3. Basu, M. et al. Purification and characterization of human recombinant IgE-Fc fragments that bind to the human high affinity IgE receptor. J. Biol. Chem. 268, 13118–13127 ( 1993). (10.1016/S0021-9258(19)38627-2) / J. Biol. Chem. by M Basu (1993)
  4. Keown, M. B. et al. Hydrodynamic studies of a complex between the Fc fragment of human IgE and a soluble fragment of the FcεRI α-chain. Proc. Natl Acad. Sci. USA 92, 1841– 1845 (1995). (10.1073/pnas.92.6.1841) / Proc. Natl Acad. Sci. USA by MB Keown (1995)
  5. Keown, M. B., Ghirlando, R., Mackay, G. A., Sutton, B. J. & Gould, H. J. Basis of the 1:1 stoichiometry of the high affinity receptor FcεRI-IgE complex. Eur. Biophys. J. 25, 471–476 ( 1997). (10.1007/s002490050062) / Eur. Biophys. J. by MB Keown (1997)
  6. Daeron, M. Fc receptor biology. Annu. Rev. Immunol. 15, 203–234 (1997). (10.1146/annurev.immunol.15.1.203) / Annu. Rev. Immunol. by M Daeron (1997)
  7. Turner, H. & Kinet, J. P. Signalling through the high-affinity IgE receptor FcεRI. Nature 402 (Suppl. B), 24–30 (1999). (10.1038/35037021) / Nature by H Turner (1999)
  8. Ravetch, J. V. & Clynes, R. A. Divergent roles for Fc receptors and complement in vivo. Annu. Rev. Immunol. 16, 421–432 (1998). (10.1146/annurev.immunol.16.1.421) / Annu. Rev. Immunol. by JV Ravetch (1998)
  9. Cookson, W. The alliance of genes and environment in asthma and allergy. Nature 402 (suppl. B), 5–11 ( 1999). (10.1038/35037002) / Nature by W Cookson (1999)
  10. Jardieu, P. M. & Fick, R. B. Jr IgE inhibition as a therapy for allergic disease. Int. Arch. Allergy Immunol. 118, 112–115 ( 1999). (10.1159/000024043) / Int. Arch. Allergy Immunol. by PM Jardieu (1999)
  11. Chang, T. W. The pharmacological basis of anti-IgE therapy. Nature Biotechnol. 18, 157–162 ( 2000). (10.1038/72601) / Nature Biotechnol. by TW Chang (2000)
  12. Garman, S. C., Kinet, J. P. & Jardetzky, T. S. Crystal structure of the human high-affinity IgE receptor. Cell 95, 951– 961 (1998). (10.1016/S0092-8674(00)81719-5) / Cell by SC Garman (1998)
  13. Nissim, A., Jouvin, M. H. & Eshhar, Z. Mapping of the high affinity Fcε-receptor binding site to the third constant region domain of IgE. EMBO J. 10, 101–107 (1991). (10.1002/j.1460-2075.1991.tb07925.x) / EMBO J. by A Nissim (1991)
  14. Keegan, A. D., Fratazzi, C., Shopes, B., Baird, B. & Conrad, D. H. Characterization of new rat anti-mouse IgE monoclonals and their use along with chimeric IgE to further define the site that interacts with FcεRII and FcεRI. Mol. Immunol. 28, 1149–1154 (1991). (10.1016/0161-5890(91)90030-N) / Mol. Immunol. by AD Keegan (1991)
  15. Presta, L. et al. The binding site on human immunoglobulin E for its high affinity receptor. J. Biol. Chem. 269, 26368– 26373 (1994). (10.1016/S0021-9258(18)47203-1) / J. Biol. Chem. by L Presta (1994)
  16. Henry, A. 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, 15568–15578 (1997). (10.1021/bi971299+) / Biochemistry by AJ Henry (1997)
  17. Granato, D. A. & Neeser, J. R. Effect of trimming inhibitors on the secretion and biological activity of a murine IgE monoclonal antibody. Mol. Immunol. 24, 849– 855 (1987). (10.1016/0161-5890(87)90187-8) / Mol. Immunol. by DA Granato (1987)
  18. Letourneur, O., Sechi, S., Willette-Brown, J., Robertson, M. W. & Kinet, J. P. Glycosylation of human truncated FcεRI α-chain is necessary for efficient folding in the endoplasmic reticulum. J. Biol. Chem. 270, 8249– 8256 (1995). (10.1074/jbc.270.14.8249) / J. Biol. Chem. by O Letourneur (1995)
  19. Kanellopoulos, J. M., Liu, T. Y., Poy, G. & Metzger, H. Composition and subunit structure of the cell receptor for immunoglobulin E. J. Biol. Chem. 255, 9060–9066 (1980). (10.1016/S0021-9258(19)70527-4) / J. Biol. Chem. by JM Kanellopoulos (1980)
  20. Robertson, M. W. Phage and Escherichia coli expression of the human high affinity immunoglobulin E receptor α-subunit ectodomain. Domain localization of the IgE-binding site. J. Biol. Chem. 268, 12736– 12743 (1993). (10.1016/S0021-9258(18)31450-9) / J. Biol. Chem. by MW Robertson (1993)
  21. Maxwell, K. F. et al. Crystal structure of the human leukocyte Fc receptor, FcγRIIa. Nature Struct. Biol. 6, 437– 442 (1999). (10.1038/8241) / Nature Struct. Biol. by KF Maxwell (1999)
  22. Sondermann, P., Huber, R. & Jacob, U. Crystal structure of the soluble form of the human FcγRIIb: a new member of the immunoglobulin superfamily at 1.7 Å resolution. EMBO J. 18, 1095–1103 (1999). (10.1093/emboj/18.5.1095) / EMBO J. by P Sondermann (1999)
  23. Sondermann, P., Jacob, U., Kutscher, C. & Frey, J. Characterization and crystallization of soluble human FcγRII (CD32) isoforms produced in insect cells. Biochemistry 38, 8469– 8477 (1999). (10.1021/bi982889q) / Biochemistry by P Sondermann (1999)
  24. Sanchez, L. M., Penny, D. M. & Bjorkman, P. J. Stoichiometry of the interaction between the major histocompatibility complex-related Fc receptor and its Fc ligand. Biochemistry 38, 9471–9476 (1999). (10.1021/bi9907330) / Biochemistry by LM Sanchez (1999)
  25. Shi, J. et al. Interaction of the low-affinity receptor CD23/FcεRII lectin domain with the Fcε3-4 fragment of human immunoglobulin E. Biochemistry 36, 2112–2122 (1997). (10.1021/bi961231e) / Biochemistry by J Shi (1997)
  26. Deisenhofer, J., Colman, P. M., Epp, O. & Huber, R. Crystallographic structural studies of a human Fc fragment. II. A complete model based on a Fourier map at 3.5 Å resolution. Hoppe Seylers Z. Physiol. Chem. 357, 1421–1434 ( 1976). (10.1515/bchm2.1976.357.2.1421) / Hoppe Seylers Z. Physiol. Chem. by J Deisenhofer (1976)
  27. Harris, L. J., Larson, S. B. & McPherson, A. Comparison of intact antibody structures and the implications for effector function. Adv. Immunol. 72, 191–208 (1999). (10.1016/S0065-2776(08)60021-8) / Adv. Immunol. by LJ Harris (1999)
  28. Schreiber, S. L. Target-oriented and diversity-oriented organic synthesis in drug discovery. Science 287, 1964–1969 (2000). (10.1126/science.287.5460.1964) / Science by SL Schreiber (2000)
  29. Mallamaci, M. A. et al. Identification of sites on the human FcεRI α-subunit which are involved in binding human and rat IgE. J. Biol. Chem. 268, 22076–22083 ( 1993). (10.1016/S0021-9258(20)80650-4) / J. Biol. Chem. by MA Mallamaci (1993)
  30. Hulett, M. D., Witort, E., Brinkworth, R. I., McKenzie, I. F. & Hogarth, P. M. Identification of the IgG binding site of the human low affinity receptor for IgG FcγRII. Enhancement and ablation of binding by site-directed mutagenesis. J. Biol. Chem. 269, 15287–15293 ( 1994). (10.1016/S0021-9258(17)36604-8) / J. Biol. Chem. by MD Hulett (1994)
  31. Hulett, M. D., Witort, E., Brinkworth, R. I., McKenzie, I. F. & Hogarth, P. M. Multiple regions of human FcγRII (CD32) contribute to the binding of IgG. J. Biol. Chem. 270, 21188–21194 (1995). (10.1074/jbc.270.36.21188) / J. Biol. Chem. by MD Hulett (1995)
  32. Cook, J. P. et al. Identification of contact residues in the IgE binding site of human FcεRIα. Biochemistry 36, 15579–15588 (1997). (10.1021/bi9713005) / Biochemistry by JP Cook (1997)
  33. Hulett, M. D., Brinkworth, R. I., McKenzie, I. F. & Hogarth, P. M. Fine structure analysis of interaction of FcεRI with IgE. J. Biol. Chem. 274, 13345–13352 (1999). (10.1074/jbc.274.19.13345) / J. Biol. Chem. by MD Hulett (1999)
  34. Sayers, I. et al. Amino acid residues that influence FcεRI-mediated effector functions of human immunoglobulin E. Biochemistry 37 , 16152–16164 (1998). (10.1021/bi981456k) / Biochemistry by I Sayers (1998)
  35. Anderson, C. L., Ryan, D. H., Looney, R. J. & Leary, P. C. Structural polymorphism of the human monocyte 40 kilodalton Fc receptor for IgG. J. Immunol. 138, 2254– 2256 (1987). (10.4049/jimmunol.138.7.2254) / J. Immunol. by CL Anderson (1987)
  36. Duncan, A. R., Woof, J. M., Partridge, L. J., Burton, D. R. & Winter, G. Localization of the binding site for the human high-affinity Fc receptor on IgG. Nature 332, 563–564 (1988). (10.1038/332563a0) / Nature by AR Duncan (1988)
  37. Chappel, M. S. et al. Identification of the Fcγ-receptor class I binding site in human IgG through the use of recombinant IgG1/IgG2 hybrid and point-mutated antibodies. Proc. Natl Acad. Sci. USA 88, 9036–9040 (1991). (10.1073/pnas.88.20.9036) / Proc. Natl Acad. Sci. USA by MS Chappel (1991)
  38. Hulett, M. D., McKenzie, I. F. & Hogarth, P. M. Chimeric Fc receptors identify immunoglobulin-binding regions in human FcγRII and FcεRI. Eur. J. Immunol. 23, 640–645 ( 1993). (10.1002/eji.1830230310) / Eur. J. Immunol. by MD Hulett (1993)
  39. Jefferis, R., Lund, J. & Pound, J. D. IgG-Fc-mediated effector functions: molecular definition of interaction sites for effector ligands and the role of glycosylation. Immunol. Rev. 163, 59–76 (1998). (10.1111/j.1600-065X.1998.tb01188.x) / Immunol. Rev. by R Jefferis (1998)
  40. Keown, M. B., Henry, A. J., Ghirlando, R., Sutton, B. J. & Gould, H. J. Thermodynamics of the interaction of human immunoglobulin E with its high-affinity receptor FcεRI. Biochemistry 37, 8863–8869 (1998). (10.1021/bi972354h) / Biochemistry by MB Keown (1998)
  41. Zheng, Y., Shopes, B., Holowka, D. & Baird, B. Dynamic conformations compared for IgE and IgG1 in solution and bound to receptors. Biochemistry 31, 7446–7456 (1992). (10.1021/bi00148a004) / Biochemistry by Y Zheng (1992)
  42. Dorrington, K. J. & Bennich, H. H. Structure–function relationships in human immunoglobulin E. Immunol. Rev. 41, 3–25 (1978). (10.1111/j.1600-065X.1978.tb01458.x) / Immunol. Rev. by KJ Dorrington (1978)
  43. Otwinowski, Z. & Minor, W. in Methods in Enzymology: Macromolecular Crystallography, Part A (eds Carter, C. W. Jr & Sweet, R. M.) 307–326 (Academic, New York, 1997). (10.1016/S0076-6879(97)76066-X) / Methods in Enzymology: Macromolecular Crystallography, Part A by Z Otwinowski (1997)
  44. Collaborative Computational Project No. 4. The CCP4 Suite: Programs for Protein Crystallography. Acta Crystallogr. D 50, 760–763 ( 1994). (10.1107/S0907444994003112) / Acta Crystallogr. D by Collaborative Computational Project No. 4. (1994)
  45. Kissinger, C. R., Gehlhaar, D. K. & Fogel, D. B. Rapid automated molecular replacement by evolutionary search. Acta Crystallogr. D 55, 484– 491 (1999). (10.1107/S0907444998012517) / Acta Crystallogr. D by CR Kissinger (1999)
  46. Harris, L. J., Larson, S. B., Hasel, K. W. & McPherson, A. Refined structure of an intact IgG2a monoclonal antibody. Biochemistry 36, 1581–1597 ( 1997). (10.1021/bi962514+) / Biochemistry by LJ Harris (1997)
  47. Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110–119 (1991). (10.1107/S0108767390010224) / Acta Crystallogr. A by TA Jones (1991)
  48. Brunger, A. T. et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905–921 (1998). (10.1107/S0907444998003254) / Acta Crystallogr. D by AT Brunger (1998)
  49. Kraulis, P. J. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946 –950 (1991). (10.1107/S0021889891004399) / J. Appl. Crystallogr. by PJ Kraulis (1991)
  50. Nicholls, A., Sharp, K. A. & Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet. 11, 281–296 (1991). (10.1002/prot.340110407) / Proteins Struct. Funct. Genet. by A Nicholls (1991)
Dates
Type When
Created 23 years ago (July 26, 2002, 4:45 a.m.)
Deposited 2 years, 3 months ago (May 16, 2023, 10:02 p.m.)
Indexed 3 days, 15 hours ago (Aug. 21, 2025, 1:48 p.m.)
Issued 25 years, 1 month ago (July 1, 2000)
Published 25 years, 1 month ago (July 1, 2000)
Published Print 25 years, 1 month ago (July 1, 2000)
Funders 0

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@article{Garman_2000, title={Structure of the Fc fragment of human IgE bound to its high-affinity receptor FcεRIα}, volume={406}, ISSN={1476-4687}, url={http://dx.doi.org/10.1038/35018500}, DOI={10.1038/35018500}, number={6793}, journal={Nature}, publisher={Springer Science and Business Media LLC}, author={Garman, Scott C. and Wurzburg, Beth A. and Tarchevskaya, Svetlana S. and Kinet, Jean-Pierre and Jardetzky, Theodore S.}, year={2000}, month=jul, pages={259–266} }