The Biochemistry And Signaling Properties Of Egfr

ErbB receptors exhibit conserved structural similarity and domain topography (Fig. 1). They contain an extracellular ligand-binding region, which consists of two cysteine-rich domains, and is responsible for ligand-induced receptor dimerization. This

Fig. 1. The domain topography of EGFR. The receptor contains cysteine-rich domains (CRDs) in the extracellular region, which contribute to ligand binding. The transmembrane region contains hy-drophobic amino acids, as is the case with other cell surface receptors. Within the intracellular region lies the kinase domain, which facilitates transphorylation of the receptor upon ligand-induced dimer-ization, at distinct tyrosine residues within the C-terminal tail. Phosphorylation of these residues leads to the recruitment of SH2 domain-containing adaptor molecules and enzymes that mediate downstream signaling events. This can lead to cellular growth and proliferation, as well as cell survival via antiapoptotic signaling. EGFR mutations found in NSCLC cluster within the kinase domain, and affect the phosphorylation status of the receptor.

Fig. 1. The domain topography of EGFR. The receptor contains cysteine-rich domains (CRDs) in the extracellular region, which contribute to ligand binding. The transmembrane region contains hy-drophobic amino acids, as is the case with other cell surface receptors. Within the intracellular region lies the kinase domain, which facilitates transphorylation of the receptor upon ligand-induced dimer-ization, at distinct tyrosine residues within the C-terminal tail. Phosphorylation of these residues leads to the recruitment of SH2 domain-containing adaptor molecules and enzymes that mediate downstream signaling events. This can lead to cellular growth and proliferation, as well as cell survival via antiapoptotic signaling. EGFR mutations found in NSCLC cluster within the kinase domain, and affect the phosphorylation status of the receptor.

is followed by a hydrophobic transmembrane region and an intracellular region that consists of the kinase domain as well as a C-terminal tail that, upon phosphorylation of key tyrosine residues, serves as a docking site for canonical interacting partners.

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