Crystal structures of human NSDHL and development of its novel inhibitor with the potential to suppress EGFR activity.

In this study, we reported two X-ray crystal structures of human NSDHL, which revealed a detailed description of the coenzyme-binding site and the unique conformational change upon the binding of a coenzyme. A structure-based virtual screening and biochemical evaluation were performed and identified a novel inhibitor for NSDHL harboring suppressive activity towards EGFR. In EGFR-driven human cancer cells, treatment with the potent NSDHL inhibitor enhanced the antitumor effect of an EGFR kinase inhibitor. Overall, these findings could serve as good platforms for the development of therapeutic agents against NSDHL-related diseases. PMID: 32140747 [PubMed - as supplied by publisher]

https://www.ncbi.nlm.nih.gov/pubmed/32140747?dopt=Abstract

Source: Cellular and Molecular Life Sciences : CMLS - March 4, 2020 Category: Cytology Authors: Kim DG, Cho S, Lee KY, Cheon SH, Yoon HJ, Lee JY, Kim D, Shin KS, Koh CH, Koo JS, Choi Y, Lee HH, Oh YK, Jeong YS, Chung SJ, Baek M, Jung KY, Lim HJ, Kim HS, Park SJ, Lee JY, Lee SJ, Lee BJ Tags: Cell Mol Life Sci Source Type: research