Structure and clinical relevance of the epidermal growth factor receptor in human cancer.

ABSTRACT:

Purpose

To review the recent advances in the atomic-level understanding of the epidermal growth factor receptor (EGFR) tyrosine kinase (TK). We aim to highlight the current and future importance of these studies for the understanding and treatment of malignancies where EGFR-TK is improperly activated.

Methods

The analysis was conducted on published crystal structures deposited in the Protein Data Bank (www.pdb.org) using the program O.

Results

In this review we emphasize how recent EGFR kinase domain crystal structures can explain the mechanisms of activation for L858R and other EGFR-TK mutations, and compare these distinct activating mechanisms with those recently described for the wild-type EGFR. We suggest an atomic-level mechanism for the poor efficacy of lapatini

SUBMITTER: Kumar A 

PROVIDER: S-EPMC3799959 | biostudies-literature | 2008 Apr

REPOSITORIES: biostudies-literature