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. 2016 Sep 21;22(35):7926–7937. doi: 10.3748/wjg.v22.i35.7926

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©The Author(s) 2016. Published by Baishideng Publishing Group Inc. All rights reserved.

This article is an open-access article which was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution Non Commercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial.

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Schematic representation of the human erbB receptors in basal condition. The extracellular portion of each receptor consists of four domains (I-IV). Both domains I and III, which are related leucine-rich segments, actively participate in ligand binding, except for those of erbB2. Domains II and IV contain numerous cysteine residues and participates in dimer formation. The kinase domain of erbB3 is kinase-impaired. The growth factor groups that bind each receptor are indicated on the top. PKD: Protein kinase domain; EGF: Epidermal growth factor; EPG: Epigen; TGFα: Transforming growth factor-α; AR: Amphiregulin; BTC: Betacellulin; HB-EGF: Heparin-binding epidermal growth-factor like growth factor; EPR: Epiregulin; Nrg-1/2/3/4: Neuregulin-1/2/3/4.