@article{open2741,
           month = {February},
           title = {Role of Cys-298 in specific recognition of glutathione by aldose reductase},
          author = {Gurprit Sekhon and Balvinder Singh and Ranvir Singh},
            year = {2021},
           pages = {1--9},
            note = {Copyright of this article belongs to OPEN ACCESS},
         journal = {JOURNAL OF BIOMOLECULAR STRUCTURE \& DYNAMICS},
        keywords = {Aldose reductase; diabetes; glutathione; molecular dynamics; polyol pathway},
             url = {http://crdd.osdd.net/open/2741/},
        abstract = {Aldose reductase (AR) is an NADPH-dependent oxidoreductase that is well-studied for its role in Diabetes Mellitus. Glutathione conjugated aldehydes are efficiently catalysed by AR. We have employed molecular dynamics simulations to investigate the dynamics of a glutathione analog, {\ensuremath{\gamma}}-glutamyl-S-(1,2-di-carboxyethyl)-cysteinyl-glycine (DCEG), into the binding pocket of AR. Study revealed that backbone nitrogens of Ala-299 and Leu-300 form a tiny pocket gated by thiol group of Cys-298. The glycine moiety of DCEG was able to displace the thiol group of Cys-298 to make hydrogen bond interactions with backbone of Ala-299, Leu-300, and Leu-301. This study provides the details of the dynamic interactions of DCEG in the binding pocket of AR, and shall aid in the design/discovery of differential inhibitors against AR.Communicated by Ramaswamy H. Sarma.}
}