Huang, Kuan-Wei; Hsu, Kai-Cheng; Chu, Lee-Ya; Yang, Jinn-Moon; Yuan, Hanna S.; Hsiao, Yu-Yuan published the artcile< Identification of Inhibitors for the DEDDh Family of Exonucleases and a Unique Inhibition Mechanism by Crystal Structure Analysis of CRN-4 Bound with 2-Morpholin-4-ylethanesulfonate (MES)>, Electric Literature of 112-63-0, the main research area is DEDDh exonuclease inhibitor identification; RNase T inhibitor identification; crystal structure exonuclease CRN4 MES complex; Lassa virus NP exonuclease inhibitor identification.
The DEDDh family of 3’→5′-exonucleases plays essential roles in DNA and RNA metabolism in all kingdoms of life. Several viral and human DEDDh exonucleases can serve as antiviral drug targets due to their critical roles in virus replication. Here, using RNase T and CRN-4 exonuclease as the model systems, the authors identified potential inhibitors for DEDDh exonucleases. The authors further showed that 2 of the inhibitors (ATA and PV6R) indeed inhibited the exonuclease activity of the viral protein, NP exonuclease of Lassa fever virus in vitro. Moreover, the authors determined the crystal structure of CRN-4 in complex with MES that revealed a unique inhibition mechanism by inducing the general base His-179 to shift out of the active site. These results not only provided the structural basis for the inhibition mechanism but also suggested potential lead inhibitors for DEDDh exonucleases that may pave the way for designing nuclease inhibitors for biochem. and biomedical applications.
Journal of Medicinal Chemistry published new progress about Crystal growth. 112-63-0 belongs to class esters-buliding-blocks, and the molecular formula is C19H34O2, Electric Literature of 112-63-0.
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