EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization.

doi:10.1016/s1097-2765(03)00047-9

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Article

EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization.

Molecular cell - 1 Feb 2003

Ferguson Kathryn M, Berger Mitchell B, Mendrola Jeannine M, Cho Hyun Soo, Leahy Daniel J, Lemmon Mark A

Abstract excerpt

Epidermal growth factor (EGF) receptor is the prototype of the ErbB (HER) family receptor tyrosine kinases (RTKs), which regulate cell growth and differentiation and are implicated in many human cancers. EGF activates its receptor by inducing dimerization of the 621 amino acid EGF receptor extracellular region. We describe the 2.8 A resolution crystal structure of this entire extracellular region (sEGFR) in an...

Topics

Crystallography, X-Ray
Dimerization
Epidermal Growth Factor
ErbB Receptors
Humans
Hydrogen-Ion Concentration
In Vitro Techniques
Models, Molecular
Mutation
Protein Conformation
Protein Structure, Tertiary
Recombinant Proteins

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PMID: 12620237
DOI: 10.1016/s1097-2765(03)00047-9

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