Characterization of structural determinants of granzyme B reveals potent mediators of extended substrate specificity.

@article{Ruggles2004CharacterizationOS,
  title={Characterization of structural determinants of granzyme B reveals potent mediators of extended substrate specificity.},
  author={Sandra Waugh Ruggles and Robert Fletterick and Charles S. Craik},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 29},
  pages={30751-9}
}
Granzymes are trypsin-like serine proteases mediating apoptotic cell death that are composed of two genetically distinct subfamilies: granzyme A-like proteases resemble trypsin in their active site architecture, while granzyme B-like proteases are quite distinct. Granzyme B prefers substrates containing P4 to P1 amino acids Ile/Val, Glu/Met/Gln, Pro/Xaa, and aspartic acid N-terminal to the proteolytic cleavage. By investigating the narrow extended specificity of the granzyme B-like proteases… CONTINUE READING
9 Citations
2 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-9 of 9 extracted citations

References

Publications referenced by this paper.
Showing 1-2 of 2 references

Fmoc Solid Phase Synthesis: a Practical Approach

  • C. Chan, D. P. White
  • 2000

Variants of Granzyme B with Unique Extended Specificity

  • A. R. Rezaie, C. T. Esmon
  • Eur. J. Biochem. 242,
  • 1996

Similar Papers

Loading similar papers…