The Crystal Structure of Nα-p-tosyl-lysyl Chloromethylketone-Bound Oligopeptidase B from Serratia Proteamaculans Revealed a New Type of Inhibitor Binding

The Crystal Structure of Nα-p-tosyl-lysyl Chloromethylketone-Bound Oligopeptidase B from Serratia Proteamaculans Revealed a New Type of Inhibitor Binding

A covalent serine protease inhibitor—Na-p-Tosyl-Lysyl Chloromethylketone (TCK) is a modified lysine residue tosylated at the N-terminus and chloromethylated at the C-terminus, one molecule of which is capable of forming two covalent bonds with both Ser and His catalytic residues, was co-crystallized...

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Bibliographic Details
Main Authors: Vladimir I. Timofeev, Dmitry E. Petrenko, Yulia K. Agapova, Anna V. Vlaskina, David M. Karlinsky, Anna G. Mikhailova, Inna P. Kuranova, Tatiana V. Rakitina
Format: article
Language:EN
Published: MDPI AG 2021
Subjects:
prolyloligopeptidase
oligopeptidase B
crystal structure
intermediate state
serine protease
chloromethylketone inhibitors
Crystallography
QD901-999
Online Access:https://doaj.org/article/7504dffdaa2e4f73933f2fbd6cbe21c1
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https://doaj.org/article/7504dffdaa2e4f73933f2fbd6cbe21c1

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