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EGFR: Tale of the C‐terminal tail
Author(s) -
Gajiwala Ketan S.
Publication year - 2013
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.2283
Subject(s) - protein kinase domain , terminal (telecommunication) , microbiology and biotechnology , kinase , mutagenesis , biophysics , chemistry , biochemistry , biology , mutation , computer science , telecommunications , mutant , gene
The carboxy terminal tail of epidermal growth factor receptor (EGFR) plays a critical role in the regulation of the enzyme activity of the kinase. There is a good structural model for the mechanism by which the C‐terminal tail proximal to the kinase domain contributes to the negative regulation of the activity. Its conformation in the active state, conversely, has remained elusive due to its dynamic nature. A recently published structure of EGFR kinase domain shows the conformation of the proximal C‐terminal tail in the active kinase. Analysis of this conformational state of the C‐terminal tail is presented, and some of the mutagenesis data is revisited. © 2013 The Protein Society