A structural explanation for the recognition of tyrosine-based endocytotic signals

Science

Volumn 282, Issue 5392, 1998, Pages 1327-1332

  Owen, David J ^a   Evans, Philip R ^a  

^a MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACE PROTEIN; TYROSINE;

ARTICLE; CAENORHABDITIS ELEGANS; DROSOPHILA; ENDOCYTOSIS; HUMAN; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE; RECEPTOR BINDING; SIGNAL TRANSDUCTION;

EID: 0032514874     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.282.5392.1327     Document Type: Article

References (35)

1. T. Kirchhausen, J. S. Bonifacino, H. Riezman, Curr. Opin. Cell Biol. 9, 488 (1997).
2. J. Schlessinger and A. Ullrich, Neuron 9, 383 (1992).
3. W. S. Chen et al., Cell 59, 33 (1989).
4. A. Wells et al., Science 247, 962 (1990).
5. S. L. Schmid, Annu. Rev. Biochem. 66, 511 (1997).
6. P. Wigge and H. T. McMahon, Trends Neurosci. 21, 339 (1998).
7. W. Boll et al., EMBO J. 15, 5789 (1996).
8. H. Ohno et al., Science 269, 1872 (1995).
9. 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; and Y, Tyr.
10. I. Rapoport, Y. Chen, C. P. Cupers, S. E., Shoelson, T. Kirchhausen, EMBO J. 17, 2148 (1998).
11. M. Foti et al., J. Cell Biol. 139, 37 (1997).
12. S. Grzesiek, S. J. Stahl, P. T. Wingfield, A. Bax, Biochemistry 35, 10256 (1996).
13. 2-terminus, so the derivatives were sufficiently isomorphous to the peptide complex to be used in phase calculations (Fig. 2A). The shorter construct (residues 158 to 435) used for the DYQRLN peptide complex did not crystallize in the absence of peptide; this isomorphous complex was refined starting with a model of the first complex with the peptide removed (Fig. 2B). Although the R factors are rather high, presumably because of the high overall B factor and the disordered regions, the experimental maps and the details of the peptide binding are clear (Fig. 2). The coordinates and structure factors have been deposited in the Protein Data Bank with codes 1BW8 (EGFR peptide complex) and 1BXX (TGN38 complex).
14. A. Sorkin, M. Mazzoti, T. Sorkina, L. Scotto, L. Beguinot, J. Biol. Chem. 271, 13377 (1996).
15. K. Bos, C. Wraight, K. K. Stanley, EMBO J. 12, 2219 (1993).
16. J. S. Humphrey, P. J. Peters, L. C. Yuan, J. S. Bonifacino, J. Cell Biol. 120, 1123 (1993).
17. J. F. Collawn et al., Cell 63, 1061 (1990).
18. E. D. Lowe et al., EMBO J. 16, 6646 (1997).
19. M.-P. Egloff et al., ibid., p. 1876.
20. H. Ohno, M.-C. Fournier, G. Poy, J. S. Bonifacino, J. Biol. Chem. 271, 29009 (1996).
21. Z. Songyang et al., Cell 72, 767 (1993).
22. G. Waksman et al., Nature 358, 646 (1992).
23. A. Nesterov, R. C. Kurten, G. N. Gill, J. Biol. Chem. 270, 6320 (1995).
24. A. Sorkin, T. McKinsey, W. Shih, T. Kirchhausen, G. Carpenter, ibid., p. 619.
25. D. Murray, N. Ben-Tal, B. Honig, S. McLaughlin, Structure 5, 985 (1997).
26. A. G. W. Leslie, in Joint CCP4 and CSF-EACMB Newsletter on Protein Crystallography No. 26 (SERC, Daresbury Laboratory, Warrington, UK, 1992).
27. Collaborative Computational Project, Acta Crystallogr. D50, 760 (1994).
28. E. de la Fortelle and G. Bricogne, Methods Enzymol. 276, 472 (1997).
29. J. P. Abrahams and A. G. W. Leslie, Acta Crystallogr. D52, 30 (1996).
30. T. A. Jones, J. Y. Zou, S. W. Cowan, M. Kjeldgaard, ibid. A47, 110 (1991).
31. G. N. Murshudov, A. A. Vagin, E. J. Dodson, ibid. D53, 240 (1997).
32. R. M. Esnouf, J. Mol. Graphics 15, 133 (1997).
33. A. Nicholls, K. A. Sharp, B. Honig, Proteins 11, 281 (1991).
34. K. Diederichs and P. A. Karplus, Nature Struct. Biol. 4, 269 (1997).
35. We thank M. S. Robinson for the rat μ2 clone, A. J. McCoy and the staff of SRS Daresbury for assistance in data collection, L. LoConte and J. Janin for the surface area calculations, and H. T. McMahon, M. S. Robinson, and M. E. M. Noble for discussions.