Kinetic and thermodynamic effects of phosphorylation on p53 binding to MDM2

• Main Authors: Yadahalli, Shilpa, Neira, José L., Johnson, Christopher M., Tan, Yaw Sing, Rowling, Pamela J. E., Chattopadhyay, Anasuya, Itzhaki, Laura S., Verma, Chandra Shekhar
• Other Authors: School of Biological Sciences
• Format: Article
• Language: English
• Published: 2019
• Subjects: Phosphorylation; DRNTU::Science::Biological sciences; Thermodynamic Effects
• Online Access: https://hdl.handle.net/10356/85410; http://hdl.handle.net/10220/48215
• Institution: Nanyang Technological University

p53 is frequently mutated in human cancers. Its levels are tightly regulated by the E3 ubiquitin ligase MDM2. The complex between MDM2 and p53 is largely formed by the interaction between the N-terminal domain of MDM2 and the N-terminal transactivation (TA) domain of p53 (residues 15–29). We investi...