1xoi
Human Liver Glycogen Phosphorylase A complexed with Chloroindoloyl glycine amideHuman Liver Glycogen Phosphorylase A complexed with Chloroindoloyl glycine amide
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe synthesis, in vitro, and in vivo biological characterization of a series of achiral 5-chloroindoloyl glycine amide inhibitors of human liver glycogen phosphorylase A are described. Improved potency over previously reported compounds in cellular and in vivo assays was observed. The allosteric binding site of these compounds was shown by X-ray crystallography to be the same as that reported previously for 5-chloroindoloyl norstatine amides. 5-Chloroindoloyl glycine amide inhibitors of glycogen phosphorylase: synthesis, in vitro, in vivo, and X-ray crystallographic characterization.,Wright SW, Rath VL, Genereux PE, Hageman DL, Levy CB, McClure LD, McCoid SC, McPherson RK, Schelhorn TM, Wilder DE, Zavadoski WJ, Gibbs EM, Treadway JL Bioorg Med Chem Lett. 2005 Jan 17;15(2):459-65. PMID:15603973[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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