Disruption of the intramolecular interaction between human lung cancer-related EGFR kinase domain and carboxy-terminal tail by intra-Tyr1016 phosphorylation or extra-peptidic competitors
Key Points
Disruption of intramolecular interactions affects function of the EGFR kinase domain, crucial for lung cancer development.
Key evidence showed that Tyr1016 phosphorylation significantly alters the interaction dynamics of EGFR.
Analysis of phosphorylation effects and competitor interactions highlights detailed mechanistic insights into cancer signaling pathways.
Understanding these interactions may enable the identification of new therapeutic strategies against lung cancer.
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Disruption of the intramolecular interaction between human lung cancer-related EGFR kinase domain and carboxy-terminal tail by intra-Tyr1016 phosphorylation or extra-peptidic competitors | Synapse