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Laminin receptor protein (67LR) is derived from a 37 kDa precursor (37LRP or RPSA) through post-translational modification, typically by fatty acid acylation and dimerization. The mature 67 kDa form localizes to the cell surface where it binds laminin, a key extracellular matrix protein, to mediate cell adhesion, signal transduction, and cellular migration. It is overexpressed in many cancers and correlates with metastatic potential, serving as a receptor not only for laminin but also elastin, prion proteins, and certain viruses (e.g., Sindbis, Dengue), underlining its role in infection and neurodegenerative disease. The precursor has essential ribosomal functions, including RNA processing and protein translation, making this receptor a multifunctional protein strongly conserved across species. Therapeutic targeting of 67LR is under active investigation, primarily for anti-cancer and anti-viral strategies, though its widespread biological roles present challenges for drug specificity and safety.
Inhibition of laminin binding (block cell adhesion/migration and metastasis); Disruption of peptide G domain interactions; Modulation of cell survival/proliferation (potential anti-tumor activity)
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