A preliminary neutron Laue diffraction study of the aspartic proteinase endothiapepsin.
Until now, no aspartic proteinase has been subjected to a successful neutron diffraction analysis, owing to the limited size of the crystals. However, the recent development of the neutron Laue technique at ILL and EMBL (Grenoble) has allowed the collection of data to 2.2 A on a complex of endothiapepsin with a transition-state analogue. The objective is to define the positions of the protons at the active site by refinement using the neutron data. In line with work on serine proteinases, where neutron diffraction has provided some of the most definitive data on the catalytic mechanism, it is expected that this work will have a major significance for studies of the aspartic proteinase enzymes.
Cooper
J B
JB
Division of Biochemistry, School of Biological Sciences, University of Southampton, Bassett Crescent East, Southampton, SO16 7PX, England. jbc2@soton.ac.uk
Myles
D A
DA
D016282:Aspartic Acid Endopeptidases / Q000037:antagonists & inhibitors / Q000737:chemistry*; D001665:Binding Sites; D003461:Crystallography / Q000379:methods; D009502:Neutrons; D009842:Oligopeptides / Q000737:chemistry; D011480:Protease Inhibitors / Q000737:chemistry; D011506:Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry; D012542:Scattering, Radiation
D009842:Oligopeptides; D011480:Protease Inhibitors; D011506:Proteins; C046598:H 261; D016282:Aspartic Acid Endopeptidases; C042466:Endothia aspartic proteinase