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Scanned: 1782 Evaluated: 279 Selected: 72 |
| MCS PRIME POISON POLLUTION | ||||||||
Bbc28-004 | A covalent irreversible inhibitor binds in two mutually exclusive conformations to the active-site cysteine residue of human aldehyde dehydrogenase 1A3 | |||||||
| Quote: | Biochemical and biophysical tests confirmed that Z34 acts as a time-dependent, covalent, and irreversible binder to the active-site cysteine. In this work, we determined the Cryo-EM structure of the ALDH1A3-Z34 complex at 2.26 resolution, confirming the covalent attachment to the catalytic cysteine of Z34. Notably, two mutually exclusive covalent binding modes were observed: one occupying the substrate-binding pocket and the other the cofactor-binding region. Z34 displayed unexpected binding modes within the active site and holds promise as a lead compound for future drug development. | |||||||
| Article: | https://www.biorxiv.org/content/10.64898/2026.07.14.738401v1 | |||||||
| Search Similar: | Brave Mojeek Startpage Dogpile Bing Googl Lycos Utub Yaho | |||||||
| Search Authors: | Daniela Covaleda David Vizarraga Tulsi Upadhyay Jiyun Zhu Daniel Abegg Raquel Pequerul Martn Hugo Alexander Adibekian Ignacio Fita Xavier Pars Francesc Xavier Avils Matthew Boggyo Jaume Farrs, | |||||||
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Javilk's Research Links for Week 28 Updated 07/17/2026-11:18:40 PM What interests you? What have you found? Tell me! Drop me a note to subscribe or submit something. |