Crystal structure of mouse CD1: An MHC-like fold with a large hydrophobic binding groove

Science

Volumn 277, Issue 5324, 1997, Pages 339-345

  Zeng, Z H ^a,b   Castano A R ^a,c   Segelke, B W ^a   Stura, E A ^a   Peterson, P A ^a   Wilson, I A ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b INSTITUTE OF BIOPHYSICS   (China)

^c INSTITUTO DE SALUD CARLOS III   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

CD1 ANTIGEN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2;

ANTIGEN PRESENTATION; ARTICLE; BACTERIAL CELL WALL; CRYSTAL STRUCTURE; HYDROPHOBICITY; MOUSE; MYCOBACTERIUM; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING;

ANIMALS; ANTIGEN PRESENTATION; ANTIGENS, CD1; BINDING SITES; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; GLYCOLIPIDS; HISTOCOMPATIBILITY ANTIGENS CLASS I; HISTOCOMPATIBILITY ANTIGENS CLASS II; HUMANS; HYDROGEN BONDING; LIGANDS; LIPID METABOLISM; LIPIDS; MICE; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; T-LYMPHOCYTE SUBSETS;

EID: 0030826423     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.277.5324.339     Document Type: Article

References (89)

1. A. J. McMichael et al., Eur. J. Immunol. 9, 205 (1979); F. Calabi and C. Milstein, Nature 323, 540 (1986); L. H. Martin, F. Calabi, C. Milstein, Proc. Natl. Acad. Sci. U.S.A. 83, 9154 (1986).
2. A. J. McMichael et al., Eur. J. Immunol. 9, 205 (1979); F. Calabi and C. Milstein, Nature 323, 540 (1986); L. H. Martin, F. Calabi, C. Milstein, Proc. Natl. Acad. Sci. U.S.A. 83, 9154 (1986).
3. A. J. McMichael et al., Eur. J. Immunol. 9, 205 (1979); F. Calabi and C. Milstein, Nature 323, 540 (1986); L. H. Martin, F. Calabi, C. Milstein, Proc. Natl. Acad. Sci. U.S.A. 83, 9154 (1986).
4. H. G. Rammensee, K. Falk, O. Rotzschke, Annu. Rev. Immunol. 11, 213 (1993).
5. R. N. Germain and D. H. Margulies, ibid., p. 403.
6. C. R. Wang, B. E. Loveland, K. F. Lindahl, Cell 66, 335 (1991); P. H. Gulden et al., Immunity 5, 73 (1996); L. L. Lenz, B. Dere, M. J. Bevan, ibid., p. 63.
7. C. R. Wang, B. E. Loveland, K. F. Lindahl, Cell 66, 335 (1991); P. H. Gulden et al., Immunity 5, 73 (1996); L. L. Lenz, B. Dere, M. J. Bevan, ibid., p. 63.
8. C. R. Wang, B. E. Loveland, K. F. Lindahl, Cell 66, 335 (1991); P. H. Gulden et al., Immunity 5, 73 (1996); L. L. Lenz, B. Dere, M. J. Bevan, ibid., p. 63.
9. b: A. C. Young, W. Zhang, J. C. Sacchettini, S. G. Nathenson, ibid. 76, 39 (1994). HLA-A2: P. J. Bjorkman et al., Nature 329, 506 (1987); P. J. Bjorkman et al., ibid., p. 512; D. R. Madden, D. N. Garboczi, D. C. Wiley, Cell 75, 693 (1993); E. J. Collins, D. N. Garboczi, D. C. Wiley, Nature 371, 626 (1994). HLA-B27: D. R. Madden, J. C. Gorga, J. L. Strominger, D. C. Wiley, ibid. 353, 321 (1991). HLA-Aw68: T. P. Garrett, M. A. Saper, P. J. Bjorkman, J. L. Strominger, D. C. Wiley, ibid. 342, 692 (1989); M. L. Silver, H. C. Guo, J. L. Strominger, D. C. Wiley, ibid. 360, 367 (1992); E. J. Collins, D. N. Garboczi, M. N. Karpusas, D. C. Wiley, Proc. Natl. Acad. Sci. U.S.A. 92, 1218 (1995). HLA-B53: K. J. Smith et al., Immunity 4, 215 (1996). HLA-B35: K. J. Smith et al., ibid., p. 203.
10. b: A. C. Young, W. Zhang, J. C. Sacchettini, S. G. Nathenson, ibid. 76, 39 (1994). HLA-A2: P. J. Bjorkman et al., Nature 329, 506 (1987); P. J. Bjorkman et al., ibid., p. 512; D. R. Madden, D. N. Garboczi, D. C. Wiley, Cell 75, 693 (1993); E. J. Collins, D. N. Garboczi, D. C. Wiley, Nature 371, 626 (1994). HLA-B27: D. R. Madden, J. C. Gorga, J. L. Strominger, D. C. Wiley, ibid. 353, 321 (1991). HLA-Aw68: T. P. Garrett, M. A. Saper, P. J. Bjorkman, J. L. Strominger, D. C. Wiley, ibid. 342, 692 (1989); M. L. Silver, H. C. Guo, J. L. Strominger, D. C. Wiley, ibid. 360, 367 (1992); E. J. Collins, D. N. Garboczi, M. N. Karpusas, D. C. Wiley, Proc. Natl. Acad. Sci. U.S.A. 92, 1218 (1995). HLA-B53: K. J. Smith et al., Immunity 4, 215 (1996). HLA-B35: K. J. Smith et al., ibid., p. 203.
11. b: A. C. Young, W. Zhang, J. C. Sacchettini, S. G. Nathenson, ibid. 76, 39 (1994). HLA-A2: P. J. Bjorkman et al., Nature 329, 506 (1987); P. J. Bjorkman et al., ibid., p. 512; D. R. Madden, D. N. Garboczi, D. C. Wiley, Cell 75, 693 (1993); E. J. Collins, D. N. Garboczi, D. C. Wiley, Nature 371, 626 (1994). HLA-B27: D. R. Madden, J. C. Gorga, J. L. Strominger, D. C. Wiley, ibid. 353, 321 (1991). HLA-Aw68: T. P. Garrett, M. A. Saper, P. J. Bjorkman, J. L. Strominger, D. C. Wiley, ibid. 342, 692 (1989); M. L. Silver, H. C. Guo, J. L. Strominger, D. C. Wiley, ibid. 360, 367 (1992); E. J. Collins, D. N. Garboczi, M. N. Karpusas, D. C. Wiley, Proc. Natl. Acad. Sci. U.S.A. 92, 1218 (1995). HLA-B53: K. J. Smith et al., Immunity 4, 215 (1996). HLA-B35: K. J. Smith et al., ibid., p. 203.
12. b: A. C. Young, W. Zhang, J. C. Sacchettini, S. G. Nathenson, ibid. 76, 39 (1994). HLA-A2: P. J. Bjorkman et al., Nature 329, 506 (1987); P. J. Bjorkman et al., ibid., p. 512; D. R. Madden, D. N. Garboczi, D. C. Wiley, Cell 75, 693 (1993); E. J. Collins, D. N. Garboczi, D. C. Wiley, Nature 371, 626 (1994). HLA-B27: D. R. Madden, J. C. Gorga, J. L. Strominger, D. C. Wiley, ibid. 353, 321 (1991). HLA-Aw68: T. P. Garrett, M. A. Saper, P. J. Bjorkman, J. L. Strominger, D. C. Wiley, ibid. 342, 692 (1989); M. L. Silver, H. C. Guo, J. L. Strominger, D. C. Wiley, ibid. 360, 367 (1992); E. J. Collins, D. N. Garboczi, M. N. Karpusas, D. C. Wiley, Proc. Natl. Acad. Sci. U.S.A. 92, 1218 (1995). HLA-B53: K. J. Smith et al., Immunity 4, 215 (1996). HLA-B35: K. J. Smith et al., ibid., p. 203.
13. b: A. C. Young, W. Zhang, J. C. Sacchettini, S. G. Nathenson, ibid. 76, 39 (1994). HLA-A2: P. J. Bjorkman et al., Nature 329, 506 (1987); P. J. Bjorkman et al., ibid., p. 512; D. R. Madden, D. N. Garboczi, D. C. Wiley, Cell 75, 693 (1993); E. J. Collins, D. N. Garboczi, D. C. Wiley, Nature 371, 626 (1994). HLA-B27: D. R. Madden, J. C. Gorga, J. L. Strominger, D. C. Wiley, ibid. 353, 321 (1991). HLA-Aw68: T. P. Garrett, M. A. Saper, P. J. Bjorkman, J. L. Strominger, D. C. Wiley, ibid. 342, 692 (1989); M. L. Silver, H. C. Guo, J. L. Strominger, D. C. Wiley, ibid. 360, 367 (1992); E. J. Collins, D. N. Garboczi, M. N. Karpusas, D. C. Wiley, Proc. Natl. Acad. Sci. U.S.A. 92, 1218 (1995). HLA-B53: K. J. Smith et al., Immunity 4, 215 (1996). HLA-B35: K. J. Smith et al., ibid., p. 203.
14. b: A. C. Young, W. Zhang, J. C. Sacchettini, S. G. Nathenson, ibid. 76, 39 (1994). HLA-A2: P. J. Bjorkman et al., Nature 329, 506 (1987); P. J. Bjorkman et al., ibid., p. 512; D. R. Madden, D. N. Garboczi, D. C. Wiley, Cell 75, 693 (1993); E. J. Collins, D. N. Garboczi, D. C. Wiley, Nature 371, 626 (1994). HLA-B27: D. R. Madden, J. C. Gorga, J. L. Strominger, D. C. Wiley, ibid. 353, 321 (1991). HLA-Aw68: T. P. Garrett, M. A. Saper, P. J. Bjorkman, J. L. Strominger, D. C. Wiley, ibid. 342, 692 (1989); M. L. Silver, H. C. Guo, J. L. Strominger, D. C. Wiley, ibid. 360, 367 (1992); E. J. Collins, D. N. Garboczi, M. N. Karpusas, D. C. Wiley, Proc. Natl. Acad. Sci. U.S.A. 92, 1218 (1995). HLA-B53: K. J. Smith et al., Immunity 4, 215 (1996). HLA-B35: K. J. Smith et al., ibid., p. 203.
15. b: A. C. Young, W. Zhang, J. C. Sacchettini, S. G. Nathenson, ibid. 76, 39 (1994). HLA-A2: P. J. Bjorkman et al., Nature 329, 506 (1987); P. J. Bjorkman et al., ibid., p. 512; D. R. Madden, D. N. Garboczi, D. C. Wiley, Cell 75, 693 (1993); E. J. Collins, D. N. Garboczi, D. C. Wiley, Nature 371, 626 (1994). HLA-B27: D. R. Madden, J. C. Gorga, J. L. Strominger, D. C. Wiley, ibid. 353, 321 (1991). HLA-Aw68: T. P. Garrett, M. A. Saper, P. J. Bjorkman, J. L. Strominger, D. C. Wiley, ibid. 342, 692 (1989); M. L. Silver, H. C. Guo, J. L. Strominger, D. C. Wiley, ibid. 360, 367 (1992); E. J. Collins, D. N. Garboczi, M. N. Karpusas, D. C. Wiley, Proc. Natl. Acad. Sci. U.S.A. 92, 1218 (1995). HLA-B53: K. J. Smith et al., Immunity 4, 215 (1996). HLA-B35: K. J. Smith et al., ibid., p. 203.
16. b: A. C. Young, W. Zhang, J. C. Sacchettini, S. G. Nathenson, ibid. 76, 39 (1994). HLA-A2: P. J. Bjorkman et al., Nature 329, 506 (1987); P. J. Bjorkman et al., ibid., p. 512; D. R. Madden, D. N. Garboczi, D. C. Wiley, Cell 75, 693 (1993); E. J. Collins, D. N. Garboczi, D. C. Wiley, Nature 371, 626 (1994). HLA-B27: D. R. Madden, J. C. Gorga, J. L. Strominger, D. C. Wiley, ibid. 353, 321 (1991). HLA-Aw68: T. P. Garrett, M. A. Saper, P. J. Bjorkman, J. L. Strominger, D. C. Wiley, ibid. 342, 692 (1989); M. L. Silver, H. C. Guo, J. L. Strominger, D. C. Wiley, ibid. 360, 367 (1992); E. J. Collins, D. N. Garboczi, M. N. Karpusas, D. C. Wiley, Proc. Natl. Acad. Sci. U.S.A. 92, 1218 (1995). HLA-B53: K. J. Smith et al., Immunity 4, 215 (1996). HLA-B35: K. J. Smith et al., ibid., p. 203.
17. b: A. C. Young, W. Zhang, J. C. Sacchettini, S. G. Nathenson, ibid. 76, 39 (1994). HLA-A2: P. J. Bjorkman et al., Nature 329, 506 (1987); P. J. Bjorkman et al., ibid., p. 512; D. R. Madden, D. N. Garboczi, D. C. Wiley, Cell 75, 693 (1993); E. J. Collins, D. N. Garboczi, D. C. Wiley, Nature 371, 626 (1994). HLA-B27: D. R. Madden, J. C. Gorga, J. L. Strominger, D. C. Wiley, ibid. 353, 321 (1991). HLA-Aw68: T. P. Garrett, M. A. Saper, P. J. Bjorkman, J. L. Strominger, D. C. Wiley, ibid. 342, 692 (1989); M. L. Silver, H. C. Guo, J. L. Strominger, D. C. Wiley, ibid. 360, 367 (1992); E. J. Collins, D. N. Garboczi, M. N. Karpusas, D. C. Wiley, Proc. Natl. Acad. Sci. U.S.A. 92, 1218 (1995). HLA-B53: K. J. Smith et al., Immunity 4, 215 (1996). HLA-B35: K. J. Smith et al., ibid., p. 203.
18. b: A. C. Young, W. Zhang, J. C. Sacchettini, S. G. Nathenson, ibid. 76, 39 (1994). HLA-A2: P. J. Bjorkman et al., Nature 329, 506 (1987); P. J. Bjorkman et al., ibid., p. 512; D. R. Madden, D. N. Garboczi, D. C. Wiley, Cell 75, 693 (1993); E. J. Collins, D. N. Garboczi, D. C. Wiley, Nature 371, 626 (1994). HLA-B27: D. R. Madden, J. C. Gorga, J. L. Strominger, D. C. Wiley, ibid. 353, 321 (1991). HLA-Aw68: T. P. Garrett, M. A. Saper, P. J. Bjorkman, J. L. Strominger, D. C. Wiley, ibid. 342, 692 (1989); M. L. Silver, H. C. Guo, J. L. Strominger, D. C. Wiley, ibid. 360, 367 (1992); E. J. Collins, D. N. Garboczi, M. N. Karpusas, D. C. Wiley, Proc. Natl. Acad. Sci. U.S.A. 92, 1218 (1995). HLA-B53: K. J. Smith et al., Immunity 4, 215 (1996). HLA-B35: K. J. Smith et al., ibid., p. 203.
19. b: A. C. Young, W. Zhang, J. C. Sacchettini, S. G. Nathenson, ibid. 76, 39 (1994). HLA-A2: P. J. Bjorkman et al., Nature 329, 506 (1987); P. J. Bjorkman et al., ibid., p. 512; D. R. Madden, D. N. Garboczi, D. C. Wiley, Cell 75, 693 (1993); E. J. Collins, D. N. Garboczi, D. C. Wiley, Nature 371, 626 (1994). HLA-B27: D. R. Madden, J. C. Gorga, J. L. Strominger, D. C. Wiley, ibid. 353, 321 (1991). HLA-Aw68: T. P. Garrett, M. A. Saper, P. J. Bjorkman, J. L. Strominger, D. C. Wiley, ibid. 342, 692 (1989); M. L. Silver, H. C. Guo, J. L. Strominger, D. C. Wiley, ibid. 360, 367 (1992); E. J. Collins, D. N. Garboczi, M. N. Karpusas, D. C. Wiley, Proc. Natl. Acad. Sci. U.S.A. 92, 1218 (1995). HLA-B53: K. J. Smith et al., Immunity 4, 215 (1996). HLA-B35: K. J. Smith et al., ibid., p. 203.
20. b: A. C. Young, W. Zhang, J. C. Sacchettini, S. G. Nathenson, ibid. 76, 39 (1994). HLA-A2: P. J. Bjorkman et al., Nature 329, 506 (1987); P. J. Bjorkman et al., ibid., p. 512; D. R. Madden, D. N. Garboczi, D. C. Wiley, Cell 75, 693 (1993); E. J. Collins, D. N. Garboczi, D. C. Wiley, Nature 371, 626 (1994). HLA-B27: D. R. Madden, J. C. Gorga, J. L. Strominger, D. C. Wiley, ibid. 353, 321 (1991). HLA-Aw68: T. P. Garrett, M. A. Saper, P. J. Bjorkman, J. L. Strominger, D. C. Wiley, ibid. 342, 692 (1989); M. L. Silver, H. C. Guo, J. L. Strominger, D. C. Wiley, ibid. 360, 367 (1992); E. J. Collins, D. N. Garboczi, M. N. Karpusas, D. C. Wiley, Proc. Natl. Acad. Sci. U.S.A. 92, 1218 (1995). HLA-B53: K. J. Smith et al., Immunity 4, 215 (1996). HLA-B35: K. J. Smith et al., ibid., p. 203.
21. b: A. C. Young, W. Zhang, J. C. Sacchettini, S. G. Nathenson, ibid. 76, 39 (1994). HLA-A2: P. J. Bjorkman et al., Nature 329, 506 (1987); P. J. Bjorkman et al., ibid., p. 512; D. R. Madden, D. N. Garboczi, D. C. Wiley, Cell 75, 693 (1993); E. J. Collins, D. N. Garboczi, D. C. Wiley, Nature 371, 626 (1994). HLA-B27: D. R. Madden, J. C. Gorga, J. L. Strominger, D. C. Wiley, ibid. 353, 321 (1991). HLA-Aw68: T. P. Garrett, M. A. Saper, P. J. Bjorkman, J. L. Strominger, D. C. Wiley, ibid. 342, 692 (1989); M. L. Silver, H. C. Guo, J. L. Strominger, D. C. Wiley, ibid. 360, 367 (1992); E. J. Collins, D. N. Garboczi, M. N. Karpusas, D. C. Wiley, Proc. Natl. Acad. Sci. U.S.A. 92, 1218 (1995). HLA-B53: K. J. Smith et al., Immunity 4, 215 (1996). HLA-B35: K. J. Smith et al., ibid., p. 203.
22. b: A. C. Young, W. Zhang, J. C. Sacchettini, S. G. Nathenson, ibid. 76, 39 (1994). HLA-A2: P. J. Bjorkman et al., Nature 329, 506 (1987); P. J. Bjorkman et al., ibid., p. 512; D. R. Madden, D. N. Garboczi, D. C. Wiley, Cell 75, 693 (1993); E. J. Collins, D. N. Garboczi, D. C. Wiley, Nature 371, 626 (1994). HLA-B27: D. R. Madden, J. C. Gorga, J. L. Strominger, D. C. Wiley, ibid. 353, 321 (1991). HLA-Aw68: T. P. Garrett, M. A. Saper, P. J. Bjorkman, J. L. Strominger, D. C. Wiley, ibid. 342, 692 (1989); M. L. Silver, H. C. Guo, J. L. Strominger, D. C. Wiley, ibid. 360, 367 (1992); E. J. Collins, D. N. Garboczi, M. N. Karpusas, D. C. Wiley, Proc. Natl. Acad. Sci. U.S.A. 92, 1218 (1995). HLA-B53: K. J. Smith et al., Immunity 4, 215 (1996). HLA-B35: K. J. Smith et al., ibid., p. 203.
23. b: A. C. Young, W. Zhang, J. C. Sacchettini, S. G. Nathenson, ibid. 76, 39 (1994). HLA-A2: P. J. Bjorkman et al., Nature 329, 506 (1987); P. J. Bjorkman et al., ibid., p. 512; D. R. Madden, D. N. Garboczi, D. C. Wiley, Cell 75, 693 (1993); E. J. Collins, D. N. Garboczi, D. C. Wiley, Nature 371, 626 (1994). HLA-B27: D. R. Madden, J. C. Gorga, J. L. Strominger, D. C. Wiley, ibid. 353, 321 (1991). HLA-Aw68: T. P. Garrett, M. A. Saper, P. J. Bjorkman, J. L. Strominger, D. C. Wiley, ibid. 342, 692 (1989); M. L. Silver, H. C. Guo, J. L. Strominger, D. C. Wiley, ibid. 360, 367 (1992); E. J. Collins, D. N. Garboczi, M. N. Karpusas, D. C. Wiley, Proc. Natl. Acad. Sci. U.S.A. 92, 1218 (1995). HLA-B53: K. J. Smith et al., Immunity 4, 215 (1996). HLA-B35: K. J. Smith et al., ibid., p. 203.
24. C. Nataraj et al., Int. Immunol. 8, 367 (1996).
25. F. Calabi, J. M. Jarvis, L. Martin, C. Milstein, Eur. J. Immunol. 19, 285 (1989).
26. S. A. Porcelli, Adv. Immunol. 59, 1 (1995).
27. S. P. Balk et al., Science 253, 1411 (1991).
28. S. Porcelli et al., Nature 341, 447 (1989).
29. A. R. Castaño et al., Science 269, 223 (1995).
30. E. M. Beckman et al., Nature 372, 691 (1994); A. Bendelac, Science 269, 185 (1995).
31. E. M. Beckman et al., Nature 372, 691 (1994); A. Bendelac, Science 269, 185 (1995).
32. P. A. Sieling et al., Science., p. 227.
33. T. I. Prigozy et al., Immunity 6, 187 (1997).
34. E. M. Beckman et al., J. Immunol. 157, 2795 (1996).
35. M. Sugita et al., Science 273, 349 (1996).
36. W. A. Ernst and R. L. Modlin, personal communication.
37. S. Cardell et al., J. Exp. Med. 182, 993 (1995).
38. A. Bendelac et al., Science 268, 863 (1995).
39. P. Dellabona et al., J. Exp. Med. 177, 1763 (1993).
40. S. P. Balk et al., Science 265, 259 (1994).
41. W. P. Burmeister, L. N. Gastinel, N. E. Simister, M. L. Blum, P. J. Bjorkman, Nature 372, 336 (1994); W. P. Burmeister, A. H. Huber, P. J. Bjorkman, ibid., p. 379.
42. W. P. Burmeister, L. N. Gastinel, N. E. Simister, M. L. Blum, P. J. Bjorkman, Nature 372, 336 (1994); W. P. Burmeister, A. H. Huber, P. J. Bjorkman, ibid., p. 379.
43. k: D. H. Fremont, W. A. Hendrickson, P. Marrack, J. Kappler, Science 272, 1001 (1996).
44. k: D. H. Fremont, W. A. Hendrickson, P. Marrack, J. Kappler, Science 272, 1001 (1996).
45. k: D. H. Fremont, W. A. Hendrickson, P. Marrack, J. Kappler, Science 272, 1001 (1996).
46. k: D. H. Fremont, W. A. Hendrickson, P. Marrack, J. Kappler, Science 272, 1001 (1996).
47. k: D. H. Fremont, W. A. Hendrickson, P. Marrack, J. Kappler, Science 272, 1001 (1996).
48. P. Bork, L. Holm, C. Sander, J. Mol. Biol. 242, 309 (1994).
49. b for 99 homologous Cα positions of the β2m domain. The rmsd values were calculated with SUPPOS (50) and a structure-based sequence alignment.
50. After aligning all homologous molecules on their β2m domains, the transformation necessary to align the α1α2 domains with CD1 is a 0.4° to 1° rotation and 3.9 to 11.4 Å translation for class I molecules (5), a 1.2° rotation and 8,6 Å translation for class II HLA-DR1 (23), and 1.0° rotation and 5.3 Å translation for FcRn (22). Aligning β2m on α3 requires a 170° rotation and 11.6 Å translation for CD1, 146° to 160° rotation and 12.9 to 13.6 Å translation for class I (5), 176° rotation and 13.5 Å translation for class II HLA-DR1 (23), and 159° rotation and 12.0 Å translation for FcRn (22).
51. 2.
52. The proportion of hydrophilicity and hydrophobicity was calculated by mapping a simple atom-specific atom type hydrophobicity or hydrophilicity parameter on to the molecular surface in GRASP (52).
53. A. R. Castaño and P. A. Peterson, unpublished data.
54. M. Teitell et al., J. Immunol. 158, 2143 (1997).
55. R. D. Salter et al., Nature 345, 41 (1990).
56. R. König, L. Y. Huang, R. N. Germain, ibid. 356, 796 (1992).
57. 2 for the homologous loop. The values for the rmsd's were calculated with SUPPOS (50).
58. . M. A. Saper, P. J. Bjorkman, D. C. Wiley, J. Mol. Biol. 219, 277 (1991); M. Matsumura, D. H. Fremont, P. A. Peterson, I. A. Wilson, Science 257, 927 (1992).
59. . M. A. Saper, P. J. Bjorkman, D. C. Wiley, J. Mol. Biol. 219, 277 (1991); M. Matsumura, D. H. Fremont, P. A. Peterson, I. A. Wilson, Science 257, 927 (1992).
60. Pockets numbers correspond to the position of the residue in the bound peptide ligand. Residues at positions 5 and 8 point up and out of the groove. Hence, there are no pockets 5 and 8.
61. 100. The distances reported are the maximum distances meeting these criteria.
62. 2) to a 5 Å probe were deleted from the surface. Surface areas were calculated from scribed molecular surfaces in GRASP (52).
63. Van der Waals contacts are assumed between any pair of atoms with their centers closer than 4 Å, and hydrogen bonds were assigned by HBPLUS (61).
64. M. R. Jackson, E. S. Song, Y. Yang, P. A. Peterson, Proc. Natl. Acad. Sci. U.S.A. 89, 12117 (1992).
65. H. G. Ljunggren et al., Nature 346, 476 (1990).
66. J. M. LaLonde, M. A. Levenson, J. J. Roe, D. A. Bemlohr, L. J. Banaszak, J. Biol. Chem. 269, 25339 (1994).
67. D. H. Shin, J. Y. Lee, K. Y. Hwang, K. K. Kim, S. W. Suh, Structure 3, 189 (1995).
68. N. K. Vyas, M. N. Vyas, F. A. Quiocho, Proc. Natl. Acad. Sci. U.S.A. 80, 1792 (1983); N. K. Vyas, M. N. Vyas, F. A. Quicho, J. Biol. Chem. 266, 5226 (1991).
69. N. K. Vyas, M. N. Vyas, F. A. Quiocho, Proc. Natl. Acad. Sci. U.S.A. 80, 1792 (1983); N. K. Vyas, M. N. Vyas, F. A. Quicho, J. Biol. Chem. 266, 5226 (1991).
70. B. W. Segelke, A. R. Castaño, P. A. Peterson, I. A. Wilson, unpublished data. The second mCD1d1 structure determination was conducted in the presence of a hydrophobic peptide, p99 (11).
71. C. R. Wang, personal communication.
72. T. Yoshimoto and W. E. Paul, J. Exp. Med. 179, 1285 (1994).
73. P. Dellabona, E. Padovan, G. Casorati, M. Brockus, A. Lanzavecchia, ibid. 180, 1171 (1994).
74. D. J. Bacon and W. F. Andersen, J. Mol. Graph. 6, 219 (1988).
75. P. J. Kraulis, J. Appl. Crystallogr. 24, 946 (1991); E. A. Merrit and M. E. P. Murphy, Acta Crystallogr. D 50, 869 (1994).
76. P. J. Kraulis, J. Appl. Crystallogr. 24, 946 (1991); E. A. Merrit and M. E. P. Murphy, Acta Crystallogr. D 50, 869 (1994).
77. F. M. D. Villieux, DEMON program suite Manual (Grenoble, France, 1993).
78. UCSF MGL, UCSF MidasPlus User's Manual (School of Pharmacy, University of California at San Francisco, San Francisco, 1995).
79. B. Honig and A. Nicholls, Science 268, 1144 (1995).
80. 6 tag. This construct was cloned into a pRMHa-3 vector and cotransfected with a mouse β2m-pRMHa-3 construct into D. melanogaster SC2 cells (11). Stable transfectants of CD1 and β2m were established, and secreted CD1-β2m complexes were isolated at room temperature by affinity chromatography on a Ni-NTA column (Qiagen) and purified by fast-performance liquid chromatography (FPLC) Mono Q (Pharmacia) and Mono S (Pharmacia) columns, or gel filtration, to a single band on an SDS gel and concentrated to 5 to 8 mg/ml.
81. B. W. Matthews, J. Mol. Biol. 33, 491 (1968).
82. A. J. Howard et al., J. Appl. Crystallogr. 20, 383 (1987).
83. Collaborative Computational Project, Number 4, Acta Crystallogr. D 50, 760 (1994).
84. F. C. Bernstein et al., J. Mol. Biol. 112, 535 (1977).
85. A10σ peak in the native Patterson map at (0.05, 0.5, 0.5) corresponds to 4σ peak in the kappa = 180° section of the self-rotation function, indicative of a non-crystallographic pseudo twofold axis passing close to (0.0, 0.0, 0.25) and parallel to the b axis.
86. A. T. Brünger, X-PLOR, version 3.1 (Yale Univ. Press, New Haven, CT, ed. 3.1, 1992).
87. T. A. Jones, in Computational Chemistry D. Sayre, Ed. (Clarendon Press, Oxford, 1982), pp. 303-317.
88. I. K. McDonald and J. M. Thomton, J. Mol. Biol. 238, 777 (1994).
89. We thank Dr. P. J. Bjorkman for the prereleased FcRn coordinates and helpful discussions and Dr. T. Yeates for helpful discussions on molecular replacement. Supported in part by grants from the National Institutes of Health, CA-58896 (I.A.W.) and the Ministerio de Educacion y Ciencia of Spain (A.R.C.). This is publication MB-10266 from the Scripps Research Institute. The coordinates for mCD1d1 have been deposited in the Protein Data Bank (Brookhaven National Laboratory, Upton, NY) with accession code 1CD1.