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Protein stability changes of the novel p.Arg180Cys mutant A glycosyltransferase resulted in a weak A phenotype
Authors:E. J. Won  M.‐T. Thi Phan  S. Y. Lee  D.‐J. Shin  S. Chun  G. Park  S.‐K. Kim  K.‐B. Lee  H.‐J. Lee  D. Cho
Affiliation:1. Department of Laboratory Medicine, Chonnam National University Medical School, Gwangju, South Korea;2. Center for Creative Biomedical Scientists, Chonnam National University, Gwangju, South Korea;3. Department of Medical System Engineering, Gwangju Institute of Science and Technology (GIST), Gwangju, South Korea;4. Department of Companion & Laboratory Animal Science, Kongju National University, Yesan, South Korea;5. Department of Laboratory Medicine and Genetics, Samsung Medical Center, Sungkyunkwan University School of Medicine, Seoul, South Korea;6. Department of Laboratory Medicine, Chosun University College of Medicine, Gwangju, South Korea;7. Advanced Analysis Center and Green City Technology Institute, Korea Institute of Science and Technology, Seoul, South Korea;8. Department of Structural Biology, St Jude Children's Research Hospital, Memphis, TN, USA
Abstract:
A novel A subgroup allele (c.538C>T p.Arg180Cys) showing weak A phenotype was found in a 30‐year‐old Korean woman with ABO discrepancy. Using 3D structural analysis, protein stability prediction and flow cytometric analysis of ABO antigen expression on HeLa cells transfected with plasmids containing the p.Arg180Cys mutant, we found that the Arg180 residue in the loop region of the A glycosyltransferases (GTA) structure plays significant role in stabilizing its closed conformation, which is required for substrate binding and catalysis study.
Keywords:blood groups  genetics  genotyping  immunogenetics  RBC antigens and antibodies
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