title: The structure of endothiapepsin complexed with the gem-diol inhibitor PD-135,040 at 1.37 A.
abstract: The crystal structure of endothiapepsin complexed with the gem-diol inhibitor PD-135,040 has been anisotropically refined to a resolution of 1.37 A. The structure of this inhibitor complex is in agreement with previous structures of endothiapepsin gem-diol inhibitor complexes that have been used to develop proposed catalytic mechanisms. However, the increase in resolution over previous structures confirms the presence of a number of short hydrogen bonds within the active site that are likely to play an important role in the catalytic mechanism. The presence of low-barrier hydrogen bonds was indicated in a previous one-dimensional H NMR spectrum.
authors.affiliation: School of Biological Sciences, University of Southampton, Bassett Crescent East, Southampton SO16 7PX, England. leightonc@bigfoot.com
authors.forename: L
authors.initials: L
authors.lastname: Coates
authors.forename: P T
authors.initials: PT
authors.lastname: Erskine
authors.forename: S
authors.initials: S
authors.lastname: Mall
authors.forename: P A
authors.initials: PA
authors.lastname: Williams
authors.forename: R S
authors.initials: RS
authors.lastname: Gill
authors.forename: S P
authors.initials: SP
authors.lastname: Wood
authors.forename: J B
authors.initials: JB
authors.lastname: Cooper
mesh_terms: D016282:Aspartic Acid Endopeptidases / Q000037:antagonists & inhibitors* / Q000737:chemistry*; D001665:Binding Sites; D002384:Catalysis; D003460:Crystallization; D004791:Enzyme Inhibitors / Q000737:chemistry* / Q000494:pharmacology; D006860:Hydrogen Bonding; D006863:Hydrogen-Ion Concentration; D007093:Imidazoles / Q000737:chemistry* / Q000494:pharmacology*; D009682:Magnetic Resonance Spectroscopy; D009025:Morpholines / Q000737:chemistry* / Q000494:pharmacology*; D014961:X-Ray Diffraction
chemical_list: D004791:Enzyme Inhibitors; D007093:Imidazoles; D009025:Morpholines; C480723:PD-135,040; D016282:Aspartic Acid Endopeptidases; C042466:Endothia aspartic proteinase