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The Conformation of a Peptidyl Methyl Ketone Inhibitor Bound to the Human Cytomegalovirus Protease

✍ Scribed by Steven R. LaPlante; Dale R. Cameron; Norman Aubry; Pierre R. Bonneau; Robert Déziel; Chantal Grand-Maître; William W. Ogilvie; Stephen H. Kawai

Publisher
John Wiley and Sons
Year
1998
Tongue
English
Weight
148 KB
Volume
37
Category
Article
ISSN
0044-8249

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✦ Synopsis

A weak inhibitor means faster exchange! Since the methyl ketone MK2 is a weak noncovalent peptidyl inhibitor of the human cytomegalovirus protease, exchange between the free and enzyme-bound forms is rapid. This allows for the use of transferred NOE NMR methods and molecular modeling, which show that the bound conformation of MK2 is an extended peptide. This is confirmed by the results of an X-ray crystallographic analysis of a related enzyme-inhibitor complex.

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✍ Haley, Terry M.; Angier, S. Jane; Borthwick, Alan D.; Montgomery, Douglas S.; Pu 📂 Article 📅 1998 🏛 John Wiley and Sons 🌐 English ⚖ 162 KB 👁 1 views

An investigation into the interaction between human cytomegalovirus (HCMV) protease and several b-lactams, with characterization of the resulting acylenzymes using mass spectrometry, is reported. The time dependence of the inhibitors is highlighted by making comparisons of values obtained for inhibi