Article
An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor.
Cell - 16 Jun 2006
Zhang Xuewu, Gureasko Jodi, Shen Kui, Cole Philip A, Kuriyan John
Abstract excerpt
The mechanism by which the epidermal growth factor receptor (EGFR) is activated upon dimerization has eluded definition. We find that the EGFR kinase domain can be activated by increasing its local concentration or by mutating a leucine (L834R) in the activation loop, the phosphorylation of which is not required for activation. This suggests that the kinase domain is intrinsically autoinhibited, and an...
Topics
- Allosteric Regulation
- Amino Acid Sequence
- Animals
- Crystallography, X-Ray
- Cyclin-Dependent Kinases
- Dimerization
- Enzyme Activation
- ErbB Receptors
- Humans
- Leucine
- Mice
- Models, Molecular
- Molecular Sequence Data
- Mutation
- NIH 3T3 Cells
- Phosphorylation
- Protein Conformation
- Protein Structure, Tertiary