Fig. 3.
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In summary, we have examined the inhibition of EstE5 and found that PMSF is a significant inhibitor of its esterase activity. Furthermore, we determined the crystal structure of EstE5–PMSF, in which the nucleophilic Ser144 of the catalytic triad and the sulfonyl center of PMSF form a covalent bond. The structural configuration of this NLG919 complex is similar to that of the serine proteases. The structure of EstE5–PMSF has significant implications for drug discovery efforts.
Acknowledgments
We thank H.S. Lee and his staff for assistance during the data collection at beamline 4A of the Pohang Light Source, Korea. This study was supported by the Functional Proteomics Center, 21C Frontier Program, of the Korea Ministry of Science and Technology (M108KM010031-08K1301-03111) and the Korea Science and Engineering Foundation; Grant No. (R01-2007-000-20072-0 (200 cool ). K.H. Nam is cyclin supported by the Brain Korea 21 project.
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