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Converging on proline: the mechanism of WW domain peptide recognition

Two new structures reveal the general rules of proline-rich motif recognition by WW domains and show that they are strikingly similar to those used by SH3 domains.

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Figure 1: WW domains use a mechanism of proline-rich peptide recognition similar to that of SH3 domains.
Figure 2: Specificity determinants in WW domain recognition.

References

  1. Lee, C.H., Cowburn, D. & Kuriyan, J. Methods Mol. Biol. 84, 3–31 (1998).

    CAS  PubMed  Google Scholar 

  2. Sudol, M. Oncogene 17, 1469–1474 (1998).

    Article  CAS  Google Scholar 

  3. Pawson, T. & Nash, P. Genes Dev. 14, 1027–1047 (2000).

    CAS  Google Scholar 

  4. Kay, B.K., Williamson, M.P. & Sudol, M. FASEB J. 14, 231–241 (2000).

    Article  CAS  Google Scholar 

  5. Rubin, G.M. et al. Science 287, 2204–2215 (2000).

    Article  CAS  Google Scholar 

  6. Huang, X. et al. Nature Struct. Biol. 7, 634–638 (2000).

    Article  CAS  Google Scholar 

  7. Verdecia, M.A., Bowman, M.E., Lu, K.P., Hunter, T. & Noel, J.P. Nature Struct. Biol. 7, 639–643 (2000).

    Article  CAS  Google Scholar 

  8. Macias, M.J. et al. Nature 382, 646–649 (1996).

    Article  CAS  Google Scholar 

  9. Sudol, M. Prog. Biophys. Mol. Biol. 65, 113–132 (1996).

    Article  CAS  Google Scholar 

  10. Chen, H.I. & Sudol, M. Proc. Natl. Acad. Sci. USA 92, 7819–7823 (1995).

    Article  CAS  Google Scholar 

  11. Rentschler, S. et al. Biol. Chem. 380, 431–442 (1999).

    Article  CAS  Google Scholar 

  12. Bedford, M.T., Sarbassova, D., Xu, J., Leder, P. & Yaffe, M.B. J. Biol. Chem. 275, 10359–10369 (2000).

    Article  CAS  Google Scholar 

  13. Roberts, R.G., Gardner, R.J. & Bobrow, M. Hum. Mutat. 4, 1–11 (1994).

    Article  CAS  Google Scholar 

  14. Lu, P.J., Zhou, X.Z., Shen, M. & Lu, K.P. Science 283, 1325–1328 (1999).

    Article  CAS  Google Scholar 

  15. Ho, C.K. & Shuman, S. Mol. Cell 3, 405–411 (1999).

    Article  CAS  Google Scholar 

  16. Steinmetz, E.J. Cell 89, 491–494 (1997).

    Article  CAS  Google Scholar 

  17. Creamer, T.P. Proteins 33, 218–226 (1998).

    Article  CAS  Google Scholar 

  18. Lim, W.A. & Richards, F.M. Nature Struct. Biol. 1, 221–225 (1994).

    Article  CAS  Google Scholar 

  19. Yu, H. et al. Cell 76, 933–945 (1994).

    Article  CAS  Google Scholar 

  20. Feng, S., Chen, J.K., Yu, H., Simon, J.A. & Schreiber, S.L. Science 266, 1241–1247 (1994).

    Article  CAS  Google Scholar 

  21. Lim, W.A., Richards, F.M. & Fox, R.O. Nature 372, 375–379 (1994). [published erratum appears in Nature 374, 94 (1995)].

    Article  CAS  Google Scholar 

  22. Nguyen, J.T., Turck, C.W., Cohen, F.E., Zuckermann, R.N. & Lim, W.A. Science 282, 2088–2092 (1998).

    Article  CAS  Google Scholar 

  23. Musacchio, A., Wilmanns, M. & Saraste, M. Prog. Biophys. Mol. Biol. 61, 283–297 (1994).

    Article  CAS  Google Scholar 

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Correspondence to Wendell A. Lim.

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Zarrinpar, A., Lim, W. Converging on proline: the mechanism of WW domain peptide recognition. Nat Struct Mol Biol 7, 611–613 (2000). https://doi.org/10.1038/77891

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