Open AccessThe Ins and Outs of EGFR Asymmetry
Author(s) -
Daniel J. Leahy
Publication year - 2010
Publication title -
cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 26.304
H-Index - 776
eISSN - 1097-4172
pISSN - 0092-8674
DOI - 10.1016/j.cell.2010.08.003
Subject(s) - epidermal growth factor receptor , scopus , protein subunit , biology , ligand (biochemistry) , cooperativity , receptor , microbiology and biotechnology , computational biology , genetics , biochemistry , gene , medline
The epidermal growth factor receptor (EGFR) regulates cell proliferation in many tissues. A new structure of the Drosophila EGFR presented by Alvarado et al. (2010) reveals an asymmetric dimer with the ligand bound to only one subunit. The structure provides a rationale for the receptor's negative cooperativity and necessitates a reconsideration of models for activation of human EGFR.
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