Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists

Science

Volumn 330, Issue 6007, 2010, Pages 1066-1071

  Wu, Beili ^a   Chien, Ellen Y T ^a   Mol, Clifford D ^a   Fenalti, Gustavo ^a   Liu, Wei ^b   Katritch, Vsevolod ^b   Abagyan, Ruben ^b   Brooun, Alexei ^c   Wells, Peter ^c   Bi, F Christopher ^c   Hamel, Damon J ^b   Kuhn, Peter ^a   Handel, Tracy M ^b   Cherezov, Vadim ^a   Stevens, Raymond C ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b UNIVERSITY OF CALIFORNIA SAN DIEGO   (United States)

^c PFIZER INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHEMOKINE RECEPTOR CXCR4; CHEMOKINE RECEPTOR CXCR5; CHEMOKINE RECEPTOR CXCR6; CYCLOPEPTIDE; G PROTEIN COUPLED RECEPTOR; VIRUS GLYCOPROTEIN;

ANTAGONISM; CANCER; CELL ORGANELLE; CRYSTAL STRUCTURE; DEVELOPMENTAL BIOLOGY; HUMAN IMMUNODEFICIENCY VIRUS; IMMUNE RESPONSE; INFECTIOUS DISEASE; LIGAND; MOLECULAR ANALYSIS; PEPTIDE; PROTEIN; RESOLUTION; SIGNALING;

BINDING AFFINITY; BINDING SITE; CRYSTAL STRUCTURE; DIMERIZATION; HUMAN; HUMAN IMMUNODEFICIENCY VIRUS 1; IMMUNOGLOBULIN DEFICIENCY; INFECTION; LEPIDOPTERA; LIGAND BINDING; MOLECULAR BIOLOGY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN ENGINEERING; REVIEW; STOICHIOMETRY; THERMOSTABILITY; VERRUCA VULGARIS;

HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 85027927015     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1194396     Document Type: Review

References (71)

1. M. Baggiolini, Nature 392, 565 (1998).
2. B. Moser, M. Wolf, A. Walz, P. Loetscher, Trends Immunol. 25, 75 (2004).
3. C. R. Mackay, Nat. Immunol. 2, 95 (2001).
4. Q. Ma et al., Proc. Natl. Acad. Sci. U.S.A. 95, 9448 (1998).
5. Y. R. Zou, A. H. Kottmann, M. Kuroda, I. Taniuchi, D. R. Littman, Nature 393, 595 (1998).
6. A. Müller et al., Nature 410, 50 (2001).
7. F. Balkwill, Semin. Cancer Biol. 14, 171 (2004).
8. A. Zlotnik, J. Pathol. 215, 211 (2008).
9. A. M. Fulton, Curr. Oncol. Rep. 11, 125 (2009).
10. B. A. Teicher, S. P. Fricker, Clin. Cancer Res. 16, 2927 (2010).
11. Y. Feng, C. C. Broder, P. E. Kennedy, E. A. Berger, Science 272, 872 (1996).
12. C. C. Bleul et al., Nature 382, 829 (1996).
13. E. Oberlin et al., Nature 382, 833 (1996).
14. G. J. Babcock, M. Farzan, J. Sodroski, J. Biol. Chem. 278, 3378 (2003).
15. Y. Percherancier et al., J. Biol. Chem. 280, 9895 (2005).
16. J. Wang, M. Norcross, Drug Discov. Today 13, 625 (2008).
17. V. Cherezov et al., Science 318, 1258 (2007).
18. V. P. Jaakola et al., Science 322, 1211 (2008).
19. T. Warne et al., Nature 454, 486 (2008).
20. J. H. Park, P. Scheerer, K. P. Hofmann, H. W. Choe, O. P. Ernst, Nature 454, 183 (2008).
21. M. A. Hanson et al., Structure 16, 897 (2008).
22. C. B. Roth, M. A. Hanson, R. C. Stevens, J. Mol. Biol. 376, 1305 (2008).
23. In Ballesteros-Weinstein numbering, a single most-conserved residue among the class A GPCRs is designated x.50, where x is the transmembrane helix number. All other residues on that helix are numbered relative to this conserved position.
24. Single-letter abbreviations for the amino acid residues are as follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; Y, Tyr; and x, any amino acid.
25. G. Thoma et al., J. Med. Chem. 51, 7915 (2008).
26. H. Tamamura et al., FEBS Lett. 550, 79 (2003).
27. S. J. DeMarco et al., Bioorg. Med. Chem. 14, 8396 (2006).
28. G. Moncunill et al., Mol. Pharmacol. 73, 1264 (2008).
29. Materials and methods are available as supporting material on Science Online.
30. H. Zhou, H. H. Tai, Arch. Biochem. Biophys. 373, 211 (2000).
31. P. Scheerer et al., Nature 455, 497 (2008).
32. K. P. Hofmann et al., Trends Biochem. Sci. 34, 540 (2009).
33. 7.39 may further shift the equilibrium toward protonation.
34. A. J. Vila-Coro et al., FASEB J. 13, 1699 (1999).
35. K. E. Luker, M. Gupta, G. D. Luker, FASEB J. 23, 823 (2009).
36. A. Levoye, K. Balabanian, F. Baleux, F. Bachelerie, B. Lagane, Blood 113, 6085 (2009).
37. D. Sohy et al., J. Biol. Chem. 284, 31270 (2009).
38. J. Wang, L. He, C. A. Combs, G. Roderiquez, M. A. Norcross, Mol. Cancer Ther. 5, 2474 (2006).
39. D. Sohy, M. Parmentier, J. Y. Springael, J. Biol. Chem. 282, 30062 (2007).
40. C. L. Salanga, M. O'Hayre, T. Handel, Cell. Mol. Life Sci. 66, 1370 (2009).
41. K. Balabanian et al., Blood 105, 2449 (2005).
42. B. Lagane et al., Blood 112, 34 (2008).
43. F. Fanelli, P. G. De Benedetti, J. Comput. Aided Mol. Des. 20, 449 (2006).
44. M. Filizola, Life Sci. 86, 590 (2010).
45. W. Nemoto, H. Toh, Curr. Protein Pept. Sci. 7, 561 (2006).
46. P. H. Reggio, AAPS J. 8, E322 (2006).
47. S. Vohra et al., Biochem. Soc. Trans. 35, 749 (2007).
48. N. Isik, D. Hereld, T. Jin, PLoS ONE 3, e3424 (2008).
49. O. M. Pello et al., Eur. J. Immunol. 38, 537 (2008).
50. M. P. Crump et al., EMBO J. 16, 6996 (1997).
51. C. Dealwis et al., Proc. Natl. Acad. Sci. U.S.A. 95, 6941 (1998).
52. S. K. Gupta, K. Pillarisetti, R. A. Thomas, N. Aiyar, Immunol. Lett. 78, 29 (2001).
53. I. Clark-Lewis et al., J. Leukoc. Biol. 57, 703 (1995).
54. T. N. Wells et al., J. Leukoc. Biol. 59, 53 (1996).
55. C. T. Veldkamp et al., Sci. Signal. 1, ra4 (2008).
56. A. Brelot et al., J. Virol. 73, 2576 (1999).
57. A. Brelot, N. Heveker, M. Montes, M. Alizon, J. Biol. Chem. 275, 23736 (2000).
58. Y. Kofuku et al., J. Biol. Chem. 284, 35240 (2009).
59. C. D. Paavola et al., J. Biol. Chem. 273, 33157 (1998).
60. V. Appay, A. Brown, S. Cribbes, E. Randle, L. G. Czaplewski, J. Biol. Chem. 274, 27505 (1999).
61. L. G. Czaplewski et al., J. Biol. Chem. 274, 16077 (1999).
62. R. Diskin, P. M. Marcovecchio, P. J. Bjorkman, Nat. Struct. Mol. Biol. 17, 608 (2010).
63. M. Pancera et al., Proc. Natl. Acad. Sci. U.S.A. 107, 1166 (2010).
64. P. D. Kwong et al., Nature 393, 648 (1998).
65. C. C. Huang et al., Science 317, 1930 (2007).
66. C. C. Huang et al., Science 310, 1025 (2005).
67. B. J. Doranz et al., J. Virol. 73, 2752 (1999).
68. T. E. Angel, M. R. Chance, K. Palczewski, Proc. Natl. Acad. Sci. U.S.A. 106, 8555 (2009).
69. S. Tian et al., J. Virol. 79, 12667 (2005).
70. J. Liu, A. Bartesaghi, M. J. Borgnia, G. Sapiro, S. Subramaniam, Nature 455, 109 (2008).
71. 1), 3OE0 (CXCR4-3-CVX15, C2), 3OE8 (CXCR4-2-IT1t, P1), 3OE9 (CXCR4-3-IT1t, P1), and 3OE6 (CXCR4-1-IT1t, I222).