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Tyrosine-protein kinase v-Src is a viral oncoprotein encoded by the Rous sarcoma virus v-Src gene, distinguished from its cellular counterpart c-Src by the absence of a key inhibitory phosphorylation site (Tyr527). This loss results in constitutive (always-on) kinase activity, driving abnormal cell proliferation, altered cell morphology, loss of contact inhibition, increased invasiveness, and ultimately, tumor formation. Structurally, v-Src is composed of several domains: SH3, SH2, and a catalytic kinase domain, enabling it to phosphorylate tyrosine residues on numerous substrates that control signal transduction, growth, and survival. v-Src and the Src family kinases are central to normal and malignant cellular processes, making them critical subjects for anti-cancer drug development and molecular research.
Inhibition of kinase activity (competitive ATP binding at kinase domain) Suppression of downstream proliferative and motility signaling
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