Substituted Cysteine Accessibility Method (SCAM) Analysis of Human Concentrative Nucleoside Transporter hCNT3 Reveals a Novel Discontinuous Region of Functional Importance Within the CNT Family Motif (G/A)XKX3NEFVA(Y/M/F)*
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چکیده
Concentrative Nucleoside Transporter hCNT3 Reveals a Novel Discontinuous Region of Functional Importance Within the CNT Family Motif (G/A)XKX3NEFVA(Y/M/F)* Melissa D. Slugoski§, Amy M. L. Ng, Sylvia Y. M. Yao, Colin C. Lin, Ras Mulinta, Carol E. Cass, Stephen A. Baldwin, and James D. Young‡ From the Membrane Protein Research Group, Departments of Physiology and Oncology, University of Alberta, and the Cross Cancer Institute, Edmonton, Alberta T6G 2H7, Canada and the Astbury Centre for Structural Molecular Biology, Institute of Membrane and Systems Biology, University of Leeds, Leeds LS2 9JT, United Kingdom. Running Title: hCNT3 SCAM Address correspondence to: Dr. James D. Young, Dept. of Physiology, 7-55 Medical Sciences Bldg., University of Alberta, Edmonton, Alberta, T6G 2H7, Canada. Tel.: 780-492-5895; Fax: 780-492-7566; Email: [email protected]
منابع مشابه
Substituted cysteine accessibility method (SCAM) analysis of the transport domain of human concentrative nucleoside transporter 3 (hCNT3) and other family members reveals features of structural and functional importance
The human SLC28 family of concentrative nucleoside transporter (CNT) proteins has three members: hCNT1, hCNT2, and hCNT3. Na+-coupled hCNT1 and hCNT2 transport pyrimidine and purine nucleosides, respectively, whereas hCNT3 transports both pyrimidine and purine nucleosides utilizing Na+ and/or H+ electrochemical gradients. Escherichia coli CNT family member NupC resembles hCNT1 in permeant selec...
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