D
Douglas R. Houston
Researcher at University of Edinburgh
Publications - 50
Citations - 2158
Douglas R. Houston is an academic researcher from University of Edinburgh. The author has contributed to research in topics: Chitinase & Virtual screening. The author has an hindex of 23, co-authored 46 publications receiving 1873 citations. Previous affiliations of Douglas R. Houston include University of Dundee & McGill University.
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Journal ArticleDOI
Crystal structure and binding properties of the Serratia marcescens chitin-binding protein CBP21
Gustav Vaaje-Kolstad,Douglas R. Houston,Anna H. K. Riemen,Vincent G. H. Eijsink,Daan M. F. van Aalten +4 more
TL;DR: Binding of CBP21 to chitin seems to be mediated primarily by conserved, solvent-exposed, polar side chains, as shown by 3–8-fold increases in the apparent binding constant.
Journal ArticleDOI
Structure of human chitotriosidase. Implications for specific inhibitor design and function of mammalian chitinase-like lectins.
Fabrizia Fusetti,Holger von Moeller,Douglas R. Houston,Henriëtte J. Rozeboom,Bauke W. Dijkstra,Rolf G. Boot,Johannes M. F. G. Aerts,Daan M. F. van Aalten +7 more
TL;DR: The crystal structure of the human chitotriosidase and complexes with a chitooligosaccharide and allosamidin reveal an elongated active site cleft, compatible with the binding of long chitin polymers, and explain the inactivation of the enzyme through an inherited genetic deficiency.
Journal ArticleDOI
Consensus Docking: Improving the Reliability of Docking in a Virtual Screening Context
TL;DR: This work presents a relatively straightforward method for improving the probability of identifying accurately docked poses, similar in concept to consensus scoring schemes, but combines information about predicted binding modes rather than predicted binding affinities.
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Structure-based exploration of cyclic dipeptide chitinase inhibitors
Douglas R. Houston,Bjørnar Synstad,Vincent G. H. Eijsink,Michael J. R. Stark,Ian M. Eggleston,Daan M. F. van Aalten +5 more
TL;DR: Four new CI-4 derivatives are presented in complex with chitinase B from Serratia marcescens, providing further insight into the mechanism of inhibition of chitInases by cyclic dipeptides as well as providing a new scaffold for chit inase inhibitor design.
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Structure and Ligand-induced Conformational Change of the 39-kDa Glycoprotein from Human Articular Chondrocytes
TL;DR: It is shown that HCGP39 is able to bind chitooligosaccharides with micromolar affinity, and this protein could be a lectin that binds chitin-like oligOSaccharide ligands and possibly plays a role in innate responses to chitinous pathogens, such as fungi and nematodes.