Identification of a second Nutlin-3 responsive interaction site in the N-terminal domain of MDM2 using hydrogen/deuterium exchange mass spectrometry

• Main Authors: Hernychova, Lenka, Man, Petr, Verma, Chandra, Nicholson, Jude, Sharma, Carrie-Anne, Ruckova, Eva, Teo, Jin Yuan, Ball, Kathryn, Vojtesek, Borek, Hupp, Ted R.
• Other Authors: School of Biological Sciences
• Format: Article
• Language: English
• Published: 2014
• Subjects: DRNTU::Science::Biological sciences
• Online Access: https://hdl.handle.net/10356/100967; http://hdl.handle.net/10220/19014
• Institution: Nanyang Technological University

MDM2 is a multidomain protein that functions as an E3 ubiquitin ligase, transcription repressor, mRNA-binding protein, translation factor, and molecular chaperone. The small molecule Nutlin-3 has been engineered to bind to the N-terminal hydrophobic pocket domain of MDM2. This binding of Nutlin-3 ha...