A novel family of cyclic peptide antagonists suggests that N-cadherin specificity is determined by amino acids that flank the HAV motif.

@article{Williams2000ANF,
  title={A novel family of cyclic peptide antagonists suggests that N-cadherin specificity is determined by amino acids that flank the HAV motif.},
  author={E J Williams and G. Ishmael Williams and Barbara J. Gour and Orest W. Blaschuk and Patrick Doherty},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 6},
  pages={4007-12}
}
The classical cadherins (e.g. N-, E-, and P- cadherin) are well established homophilic adhesion molecules; however, the mechanism that governs cadherin specificity remains contentious. The classical cadherins contain an evolutionarily conserved His-Ala-Val (HAV) sequence, and linear peptides harboring this motif are capable of inhibiting a variety of cadherin-dependent processes. We now demonstrate that short cyclic HAV peptides can inhibit N-cadherin function. Interestingly, the nature of the… CONTINUE READING

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