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Structural insights into cationic amino acid transport and viral receptor engagement by CAT1

Nature Communications. 2025-09; 
Lingyun Xia; Bingqian Lin; Rongfeng Zou; Yanyan Wu; Jiaying Xu; Yan Pan; Yuan Yuan; Shuo Li; Yang Yang; Xuemin Chen
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Protein and Antibody Isolation at 4 C for 2 hours. After ultracentrifugation at 100,000 g for 1 hour, the supernatant was collected and loaded onto anti-Flag M2 affinity resin (GenScript Biotech). The resin was washed with buffer containing 25 mM Tris (pH 8.0), 150 mM NaCl, and 0.06% LMNG (w/v). The protein was eluted with the wash buffer Get A Quote

摘要

Cationic amino acid transporter 1 (CAT1) transports cationic amino acids and plays pivotal roles in cancer proliferation, immune modulation, and nitric oxide metabolism. It also serves as the specific cellular receptor for certain murine leukemia viruses. Here, we report the cryo-electron microscopy (cryo-EM) structure of mammalian CAT1 in complex with its substrate ornithine and the receptor-binding domain (RBD) of Friend murine leukemia virus (FrMLV). CAT1 specifically recognizes the side-chain amino group of ornithine via residue S347 on transmembrane helix 8 (TM8), capturing the transporter in an inward-facing occluded conformation. Notably, the FrMLV RBD (frRBD) primarily engages the third extracellular lo... More

关键词

Cryoelectron microscopy, Virus-host interactions, Carrier proteins, Permeation and transport