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Discovery of non-retinoid compounds that suppress the pathogenic effects of misfolded rhodopsin in a mouse model of retinitis pigmentosa.
PLoS Biol
January 2025
Department of Pharmacology and Cleveland Center for Membrane and Structural Biology, School of Medicine, Case Western Reserve University, Cleveland, Ohio, United States of America.
Pathogenic mutations that cause rhodopsin misfolding lead to a spectrum of currently untreatable blinding diseases collectively termed retinitis pigmentosa. Small molecules to correct rhodopsin misfolding are therefore urgently needed. In this study, we utilized virtual screening to search for drug-like molecules that bind to the orthosteric site of rod opsin and improve its folding and trafficking.
View Article and Find Full Text PDFLectin-carbohydrate analysis by molecular dynamics: Parkia lectins case study.
An Acad Bras Cienc
December 2024
Universidade Federal do Ceará, Departamento de Bioquímica e Biologia Molecular, Laboratório de Moléculas Biologicamente Ativas, Rua José Aurelio Camara, s/n, 60440-970 Fortaleza, CE, Brazil.
Understanding lectin-carbohydrate interactions at the structural and molecular levels is crucial to the field of lectins, as the diverse roles and biological activities exhibited by these proteins are fundamentally linked to their specific binding to target glycoconjugates. This study aimed to apply molecular dynamics to analyze the structure and binding properties of Parkia lectins. 3D structures of Parkia platycephala and P.
View Article and Find Full Text PDFCryo-EM Structure of Recombinantly Expressed hUGDH Unveils a Hidden, Alternative Allosteric Inhibitor.
Biochemistry
January 2025
Department of Biochemistry & Molecular Biology, University of Georgia, Athens, Georgia 30602, United States.
Human UDP-glucose dehydrogenase (hUGDH) catalyzes the oxidation of UDP-glucose into UDP-glucuronic acid, an essential substrate in the Phase II metabolism of drugs. hUGDH is a hexamer that exists in an equilibrium between an active (E) state and an inactive (E) state, with the latter being stabilized by the binding of the allosteric inhibitor UDP-xylose (UDP-Xyl). The allosteric transition between E and E is slow and can be observed as a lag in progress curves.
View Article and Find Full Text PDFStructural, biophysical, and biochemical insights into C-S bond cleavage by dimethylsulfone monooxygenase.
Proc Natl Acad Sci U S A
November 2024
Department of Chemistry, University of Massachusetts, Boston, MA 02125.
Sulfur is an essential element for life. Bacteria can obtain sulfur from inorganic sulfate; but in the sulfur starvation-induced response, employ two-component flavin-dependent monooxygenases (TC-FMOs) from the and operons to assimilate sulfur from environmental compounds including alkanesulfonates and dialkylsulfones. Here, we report binding studies of oxidized FMN to enzymes involved within the enzymatic pathway responsible for converting dimethylsulfone (DMSO) to sulfite.
View Article and Find Full Text PDFA Target Class Ligandability Evaluation of WD40 Repeat-Containing Proteins.
J Med Chem
November 2024
Structural Genomics Consortium, University of Toronto, 101 College St., Toronto, ON M5G 1L7, Canada.
Target class-focused drug discovery has a strong track record in pharmaceutical research, yet public domain data indicate that many members of protein families remain unliganded. Here we present a systematic approach to scale up the discovery and characterization of small molecule ligands for the WD40 repeat (WDR) protein family. We developed a comprehensive suite of protocols for protein production, crystallography, and biophysical, biochemical, and cellular assays.
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