LAT1-4F2hc Flag & His tag Protein, Human (Detergent)

LAT1 (SLC7A5) is an essential amino acid transporter that forms a heterodimer with 4F2hc (SLC3A2). The recently resolved cryo-EM structure reveals a critical "outward-facing occluded conformation," where inhibitors bind to the classical substrate-binding pocket, with their tails specifically wedged between the substrate-binding site and transmembrane domain TM10. This provides atomic-level details for understanding its transport and inhibition mechanisms. LAT1 is not only responsible for transporting essential amino acids but also mediates the transmembrane influx of neuropathic pain drugs such as gabapentin. Additionally, by interacting with voltage-gated potassium channels (Kv1.1/Kv1.2) and sodium channels (Nav1.7), it regulates neuronal excitability and plays a central role in nociceptive transmission. LAT1 is highly expressed in various tumors, making it a potential target for anticancer drug design. At the same time, its upregulation in pain pathways of the dorsal root ganglia and spinal cord, along with its close association with mTOR signaling, the Wnt/β-catenin pathway, and T/B cell-related pain, positions it not only as a novel target for alleviating neuropathic pain (e.g., by mediating the uptake of first-line drugs) but also as a key structural foundation for developing new drugs capable of crossing the blood-brain barrier while exerting analgesic effects.