Nature Communications (Sep 2018)

Intriguing role of water in protein-ligand binding studied by neutron crystallography on trypsin complexes

  • Johannes Schiebel,
  • Roberto Gaspari,
  • Tobias Wulsdorf,
  • Khang Ngo,
  • Christian Sohn,
  • Tobias E. Schrader,
  • Andrea Cavalli,
  • Andreas Ostermann,
  • Andreas Heine,
  • Gerhard Klebe

DOI
https://doi.org/10.1038/s41467-018-05769-2
Journal volume & issue
Vol. 9, no. 1
pp. 1 – 15

Abstract

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Trypsin is a serine protease. Here the authors present the high resolution X-ray and neutron diffraction structures of uncomplexed and inhibitor bound trypsin that provide insights into the geometry of H-bonds in the active site of the enzyme and molecular dynamics simulations reveal the kinetics of ligand binding induced desolvation.