A conserved tryptophan (W91) at the barrel-lid junction modulates the packing and stability of Kunitz (STI) family of inhibitors.

@article{Majumder2015ACT,
  title={A conserved tryptophan (W91) at the barrel-lid junction modulates the packing and stability of Kunitz (STI) family of inhibitors.},
  author={Sudip Majumder and Susmita Khamrui and Ramanuj Banerjee and Pallab Bhowmik and Udayaditya Sen},
  journal={Biochimica et biophysica acta},
  year={2015},
  volume={1854 1},
  pages={55-64}
}
β-trefoil fold, consisting of a six stranded β-barrel capped at one end by a lid comprising of another six β-strands, is one of the most important folds among proteins. Important classes of proteins like Interleukins (ILs), Fibroblast Growth Factors (FGFs), Kunitz (STI) family of inhibitors etc. belong to this fold. Their core is packed by hydrophobic… CONTINUE READING