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. Author manuscript; available in PMC: 2020 Apr 1.
Published in final edited form as: Endocr Relat Cancer. 2019 Apr 1;26(4):R195–R209. doi: 10.1530/ERC-19-0009

Figure 1. Structure of the ErbB Receptor.

Figure 1.

ErbB receptors transmembrane proteins with both intracellular and extracellular domains. The extracellular domain is composed of four sub-domains, including two leucine-rich sub-domains (I and III) for ligand binding and two cysteine-rich sub-domains (II and IV) for dimerization with activated ErbB members. Inactivated ErbB receptors remain in the ‘closed’ conformation, while ErbB-2 is constitutively in the ‘open’ confirmation. The dimerization with other ligand-bound ErbB family members will lead to activate ErbB-2 for signaling. Intracellularly, ErbB receptors have a juxtamembrane region, a kinase domain, and a cytoplasmic tail that is regulated by tyrosine phosphorylation.