Structural basis of pH-dependent antibody binding by the neonatal Fc receptor

Structure

Volumn 6, Issue 1, 1998, Pages 63-73

  Vaughn, Daniel E ^a,b   Bjorkman, Pamela J ^a  

^a CALIFORNIA INSTITUTE OF TECHNOLOGY   (United States)

^b Howard Hughes Medical Institute Cold Spring Harbor Laboratory Cold Spring Harbor   (United States)

Author keywords

Histidine titration; Ordered carbohydrate; pH dependent salt bridges

Indexed keywords

ANIMALIA;

EID: 0032518373     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(98)00008-2     Document Type: Article

References (52)

1. Junghans, R.P. (1997). Finally! The Brambell receptor (FcRB). Mediator of transmission of immunity and protection from catabolism for IgG. Immunol. Res. 16, 29-57.
2. Rodewald, R. (1976). pH-dependent binding of immunoglobulins to intestinal cells of the neonatal rat. J. Cell Biol. 71, 666-670.
3. Rodewald, R. & Kraehenbuhl, J.-P. (1984). Receptor-mediated transport of IgG. J. Cell Biol. 99, S159-S164.
4. Raghavan, M., Bonagura, V.R., Morrison, S.L. & Bjorkman, P.J. (1995). Analysis of the pH dependence of the neonatal Fc receptor/immunoglobulin G interaction using antibody and receptor variants. Biochemistry 34, 14649-14657.
5. Kim, J.K., Tsen, M.F., Ghetie, V. & Ward, E.S. (1994). Identifying amino acid residues that influence plasma clearance of mouse IgG1 fragments by site directed mutagenesis. Eur. J. Immunol. 24, 542-548.
6. Kim, J.-K., Tsen, M.-F., Ghetie, V. & Ward, E.S. (1994). Catabolism of the murine IgG1 molecule: evidence that both CH2-CH3 domain interfaces are required for the persistence of IgG1 in the circulation of mice. Scand. J. Immunol. 40, 457-465.
7. Raghavan, M., Chen, M.Y., Gastinel, L.N. & Bjorkman, P.J. (1994). Identification of interaction sites in the class I MHC-related Fc receptor/immunoglobulin G complex. Immunity 1, 303-315.
8. Kim, J.-K., Tsen, M.-F., Ghetie, V. & Ward, E.S. (1994). Localization of the site of the murine IgG1 molecule that is involved in binding to the murine intestinal Fc receptor. Eur. J. Immunol. 24, 2429-2434.
9. Medesan, C., Matesoi, D., Radu, C., Ghetie, V. & Ward, E.S. (1997). Delineation of the amino acid residues involved in transcytosis and catabolism of mouse IgG. J. Immunol. 158, 2211-2217.
10. Raghavan, M. & Bjorkman, P.J. (1996). Fc receptors and their interactions with immunoglobulins. Ann. Rev. Cell Biol. 12, 181-220.
11. Deisenhofer, J. (1981). Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9-Å and 2.8-Å resolution. Biochemistry 20, 2361-2370.
12. Sauer-Eriksson, A.E., Kleywegt, G.J., Uhlen, M. & Jones, T.A. (1995). Crystal structure of the C2 fragment of streptococcal protein G in complex with the Fc domain of human IgG. Structure 3, 265-278.
13. Artandi, S.E., Calame, K.L., Morrison, S.L. & Bonagura, V.R. (1992). Monoclonal IgM rheumatoid factors bind IgG at a discontinuous epitope comprised of amino acid loops from heavy-chain constantregion domains 2 and 3. Proc. Natl. Acad. Sci. USA 89, 94-98.
14. Raghavan, M., Gastinel, L.N. & Bjorkman, P.J. (1993). The class I MHC-related Fc receptor shows pH dependent stability differences correlating with immunoglobulin binding and release. Biochemistry 32, 8654-8660.
15. Simister, N.E. & Rees, A.R. (1985). Isolation and characterization of an Fc receptor from neonatal rat small intestine. Eur. J. Immunol. 15, 733-738.
16. Simister, N.E. & Mostov, K.E. (1989). An Fc receptor structurally related to MHC class I antigens. Nature 337, 184-187.
17. Bjorkman, P.J. & Parham, P. (1990). Structure, function and diversity of class I major histocompatibility complex molecules. Ann. Rev. Biochem. 90, 253-288.
18. Burmeister, W.P., Gastinel, L.N., Simister, N.E., Blum, M.L. & Bjorkman, P.J. (1994). Crystal structure at 2.2 Å resolution of the MHC-related neonatal Fc receptor. Nature 372, 336-343.
19. Raghavan, M., Wang, Y. & Bjorkman, P.J. (1995). Effects of receptor dimerization on the interaction between the class I MHC related Fc receptor and immunoglobulin G. Proc. Natl. Acad. Sci. USA 92, 11200-11204.
20. Burmeister, W.P., Huber, A.H. & Bjorkman, P.J. (1994). Crystal structure of the complex of rat neonatal Fc receptor with Fc. Nature 372, 379-383.
21. Vaughn, D.E., Milburn, C.M., Penny, D.M., Martin, W.L, Johnson, J.L. & Bjorkman, P.J. (1997). Identification of critical IgG binding epitopes on the neonatal Fc receptor. J. Mol. Biol., in press.
22. Kleywegt, G.J. & Jones, T.A. (1995). Where freedom is given, liberties are taken. Structure 3, 535-540.
23. Laskowski, R.A., MacArthur, M.W., Hutchinson, E.G. & Thornton, J.M. (1992). Stereochemical quality of protein structure coordinates. Proteins 12, 345-364.
24. Fersht, A. (1985). Enzyme Structure and Mechanism, 2nd edition. W.H. Freeman and Company, New York.
25. Matthew, J.B., Gurd, F.R.N., Garcia-Morena E.B., Flanagan, M.A., March, K.L. & Shire, S.J. (1985). pH dependent processes in proteins. CRC Crit. Rev. Biochem. 18, 91-197.
26. Zheng, Y., Shopes, B., Holowka, D. & Baird, B. (1992). Dynamic conformations compared for IgE and IgG1 in solution and when bound to receptors. Biochemistry 31, 7446-7456.
27. Huber, A.H., Kelley, R.F., Gastinel, L.N. & Bjorkman, P.J. (1993). Crystallization and stoichiometry of binding of a complex between a rat intestinal Fc receptor and Fc. J. Mol. Biol. 230, 1077-1083.
28. Mackenzie, N. (1984). Fc receptor-mediated transport of immunoglobulin across the intestinal epithelium of the neonatal rodent. Immunol. Today 5, 364-366.
29. Popov, S., Hubbard, J.G., Kim, J.-K., Ober, B., Ghetie, V. & Ward, E.S. (1996). The stoichiometry and affinity of interaction of murine Fc fragments with the MHC class I-related receptor, FcRn. Mol. Immunol. 33, 521-530.
30. Luckow, V.A. & Summers, M.D. (1988). Trends in the development of baculovirus expression vectors. Biotechnology 6, 47-55.
31. Jenkins, N., Parekh, R.B. & James, D.C. (1996). Getting the glycosylation right: implications for the biotechnology industry. Nature Biotech. 14, 975-981.
32. Shaanan, B., Lis, H. & Sharon, N. (1991). Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose. Science 254, 862-866.
33. Wyss, D.F., et al., & Wagner, G. (1995). Conformation and function of the N-linked glycan in the adhesion domain of human CD2. Science 269, 1273-1278.
34. Ghosh, P., Amaya, M., Mellins, E. & Wiley, D.C. (1995). The structure of an intermediate in class II MHC maturation - CLIP bound to HLA-DR3. Nature 378, 457-462.
35. Brown, V.I. & Green, M.I. (1991). Molecular and cellular mechanisms of receptor-mediated endocytosis. DNA Cell Biol. 10, 399-409.
36. De Silva, D.M., Askwith, C.C. & Kaplan, J. (1996). Molecular mechanisms of iron uptake in eukaryotes. Physiol. Rev. 76, 31-47.
37. Kelley, R.F. & O'Connell, M.P. (1993). Thermodynamic analysis of an antibody functional epitope. Biochemistry 32, 6828-6835.
38. Tsumoto, K., Ogasahara, K., Ueda, Y., Watanabe, K., Yutani, K. & Kumagai, I. (1995). Role of Tyr residues in the contact region of antilysozyme monoclonal antibody HyHEL 10 for antigen binding. J. Biol. Chem. 270, 18551-18557.
39. Dall'Acqua, W., Goldman, E.R., Eisenstein, E. & Mariuzza, R.A. (1996). A mutational analysis of the binding of two different proteins to the same antibody. Biochemistry 35, 9667-9676.
40. Wells, J.A. & DeVos, A.M. (1996). Hematopoietic receptor complexes. Ann. Rev. Biochem. 65, 609-634.
41. Gastinel, L.N., Simister, N.E. & Bjorkman, P.J. (1992). Expression and crystallization of a soluble and functional form of an Fc receptor related to class I histocompatibility molecules. Proc. Natl. Acad. Sci. USA 89, 638-642.
42. Otwinowski, Z. & Minor, W. (1997). Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
43. Jones, T.A., Bergdoll, M. & Kjeldgaard, M. (1993). Crystallographic computing and modeling methods in molecular design. Springer, New York.
44. Adams, P.D., Pannu, N.S., Read, R.J. & Brünger, A.T. (1997). Cross-validated maximum likelihood enhances crystallographic simulated annealing refinement. Proc. Natl. Acad. Sci. USA 94, 5018-5023.
45. Pannu, N.S. & Read, R.J. (1996). Improved structure refinement through maximum likelihood. Acta Cryst. A 52, 659-668.
46. Brünger, A.T. (1992). Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475.
47. Brünger, A.T., Krukowski, A. & Erickson, J.W. (1990). Slow-cooling protocols for crystallographic refinement by simulated annealing. Acta Cryst. A 46, 585-593.
48. Hodel, A., Kim, S.-H. & Brünger, A.T. (1992). Model bias in macromolecular crystal structures. Acta cryst. A 48, 851-858.
49. Kleywegt, G.J. & Jones, T.A. (1996). Xdlmapman and Xdldataman: programs for reformatting, analysis and manipulation of biomacromolecular electron density maps and reflection data sets. Acta Cryst. D 52, 826-828.
50. Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
51. Merritt, E.A. & Murphy, M.E.P. (1994). Raster3D version 2.0, a program for photorealistic molecular graphics. Acta Cryst. D 50, 869-873.
52. Nicholls, A., Bharadwaj, R. & Honig, B. (1993). GRASP: graphical representation and analysis of surface properties. Biophys. J. 64, 166-170.