Structural insights into the substrate specificity and activity of ervatamins, the papain‐like cysteine proteases from a tropical plant, Ervatamia coronaria

@article{Ghosh2008StructuralII,
  title={Structural insights into the substrate specificity and activity of ervatamins, the papain‐like cysteine proteases from a tropical plant, Ervatamia coronaria},
  author={R. Ghosh and S. Chakraborty and C. Chakrabarti and J. Dattagupta and S. Biswas},
  journal={The FEBS Journal},
  year={2008},
  volume={275}
}
Multiple proteases of the same family are quite often present in the same species in biological systems. These multiple proteases, despite having high homology in their primary and tertiary structures, show deviations in properties such as stability, activity, and specificity. It is of interest, therefore, to compare the structures of these multiple proteases in a single species to identify the structural changes, if any, that may be responsible for such deviations. Ervatamin‐A, ervatamin‐B and… Expand
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