Kinetic and thermodynamic effects of phosphorylation on p53 binding to MDM2

Kinetic and thermodynamic effects of phosphorylation on p53 binding to MDM2

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...

Full description

Bibliographic Details
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: Journal 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

Internet

https://hdl.handle.net/10356/85410
http://hdl.handle.net/10220/48215

Similar Items