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

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...

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Auteurs principaux:	Johannes Schiebel, Roberto Gaspari, Tobias Wulsdorf, Khang Ngo, Christian Sohn, Tobias E. Schrader, Andrea Cavalli, Andreas Ostermann, Andreas Heine, Gerhard Klebe
Format:	article
Langue:	EN
Publié:	Nature Portfolio 2018
Sujets:	Science Q
Accès en ligne:	https://doaj.org/article/dfa101099f7848ffada5601ea4aa65b1
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spelling	oai:doaj.org-article:dfa101099f7848ffada5601ea4aa65b12021-12-02T17:31:45ZIntriguing role of water in protein-ligand binding studied by neutron crystallography on trypsin complexes10.1038/s41467-018-05769-22041-1723https://doaj.org/article/dfa101099f7848ffada5601ea4aa65b12018-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-05769-2https://doaj.org/toc/2041-1723Trypsin 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.Johannes SchiebelRoberto GaspariTobias WulsdorfKhang NgoChristian SohnTobias E. SchraderAndrea CavalliAndreas OstermannAndreas HeineGerhard KlebeNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-15 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Johannes Schiebel Roberto Gaspari Tobias Wulsdorf Khang Ngo Christian Sohn Tobias E. Schrader Andrea Cavalli Andreas Ostermann Andreas Heine Gerhard Klebe Intriguing role of water in protein-ligand binding studied by neutron crystallography on trypsin complexes
description	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.
format	article
author	Johannes Schiebel Roberto Gaspari Tobias Wulsdorf Khang Ngo Christian Sohn Tobias E. Schrader Andrea Cavalli Andreas Ostermann Andreas Heine Gerhard Klebe
author_facet	Johannes Schiebel Roberto Gaspari Tobias Wulsdorf Khang Ngo Christian Sohn Tobias E. Schrader Andrea Cavalli Andreas Ostermann Andreas Heine Gerhard Klebe
author_sort	Johannes Schiebel
title	Intriguing role of water in protein-ligand binding studied by neutron crystallography on trypsin complexes
title_short	Intriguing role of water in protein-ligand binding studied by neutron crystallography on trypsin complexes
title_full	Intriguing role of water in protein-ligand binding studied by neutron crystallography on trypsin complexes
title_fullStr	Intriguing role of water in protein-ligand binding studied by neutron crystallography on trypsin complexes
title_full_unstemmed	Intriguing role of water in protein-ligand binding studied by neutron crystallography on trypsin complexes
title_sort	intriguing role of water in protein-ligand binding studied by neutron crystallography on trypsin complexes
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/dfa101099f7848ffada5601ea4aa65b1
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_version_	1718380524854050816

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

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