Structural basis for exploring the allosteric inhibition of human kidney type glutaminase

• Published in: Oncotarget Vol. 7; no. 36; pp. 57943 - 57954
• Main Authors: Ramachandran, Sarath, Pan, Catherine Qiurong, Zimmermann, Sarah C, Duvall, Bridget, Tsukamoto, Takashi, Low, Boon Chuan, Sivaraman, J
• Format: Journal Article
• Language: English
• Published: United States Impact Journals LLC 06.09.2016
• Subjects: Allosteric Site; Antineoplastic Agents - chemistry; Antineoplastic Agents - pharmacology; Cell Proliferation; Glutaminase - antagonists & inhibitors; Glutaminase - chemistry; HEK293 Cells; Humans; Inhibitory Concentration 50; Kidney - enzymology; Kidney Neoplasms - enzymology; Molecular Conformation; Protein Binding; Protein Conformation; Research Paper; Sulfides - chemistry; Thiadiazoles - chemistry; glutaminase; allosteric inhibitors; BPTES; cancer target; CB-839

Cancer cells employ glutaminolysis to provide a source of intermediates for their upregulated biosynthetic needs. Glutaminase, which catalyzes the conversion of glutamine to glutamate, is gaining increasing attention as a potential drug target. Small-molecule inhibitors such as BPTES and CB-839, whi...