Protein stability changes of the novel p.Arg180Cys mutant A glycosyltransferase resulted in a weak A phenotype

H. S. Lee; K. M. Choi; 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

doi:10.1111/vox.12440

Protein stability changes of the novel p.Arg180Cys mutant A glycosyltransferase resulted in a weak A phenotype

H. S. Lee
, K. M. Choi
, 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^*

^*Corresponding author for this work

Department of Medicine

Chonnam National University
Sungkyunkwan University
Konkuk University
Gwangju Institute of Science and Technology
Kongju National University
Chosun University
Korea Institute of Science and Technology
St. Jude Children Research Hospital

Research output: Contribution to journal › Journal article › peer-review

6 Scopus citations

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.

Original language	English
Pages (from-to)	441-444
Number of pages	4
Journal	Vox Sanguinis
Volume	111
Issue number	4
DOIs	https://doi.org/10.1111/vox.12440
State	Published - 2016.11.1

Keywords

blood groups
genetics
genotyping
immunogenetics
RBC antigens and antibodies

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10.1111/vox.12440

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title = "Protein stability changes of the novel p.Arg180Cys mutant A glycosyltransferase resulted in a weak A phenotype",

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",

author = "Lee, \{H. S.\} and Choi, \{K. M.\} and Won, \{E. J.\} and \{Thi Phan\}, \{M. T.\} and Lee, \{S. Y.\} and Shin, \{D. J.\} and S. Chun and G. Park and Kim, \{S. K.\} and Lee, \{K. B.\} and Lee, \{H. J.\} and D. Cho",

note = "Publisher Copyright: {\textcopyright} 2016 International Society of Blood Transfusion",

year = "2016",

month = nov,

day = "1",

doi = "10.1111/vox.12440",

language = "English",

volume = "111",

pages = "441--444",

journal = "Vox Sanguinis",

issn = "0042-9007",

number = "4",

}

TY - JOUR

T1 - Protein stability changes of the novel p.Arg180Cys mutant A glycosyltransferase resulted in a weak A phenotype

AU - Lee, H. S.

AU - Choi, K. M.

AU - Won, E. J.

AU - Thi Phan, M. T.

AU - Lee, S. Y.

AU - Shin, D. J.

AU - Chun, S.

AU - Park, G.

AU - Kim, S. K.

AU - Lee, K. B.

AU - Lee, H. J.

AU - Cho, D.

PY - 2016/11/1

Y1 - 2016/11/1

N2 - 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.

AB - 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.

KW - blood groups

KW - genetics

KW - genotyping

KW - immunogenetics

KW - RBC antigens and antibodies

UR - https://www.scopus.com/pages/publications/84982293380

U2 - 10.1111/vox.12440

DO - 10.1111/vox.12440

M3 - Journal article

C2 - 27538125

AN - SCOPUS:84982293380

SN - 0042-9007

VL - 111

SP - 441

EP - 444

JO - Vox Sanguinis

JF - Vox Sanguinis

IS - 4

ER -

Protein stability changes of the novel p.Arg180Cys mutant A glycosyltransferase resulted in a weak A phenotype

Abstract

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