2021年10月
Modulation of the carbohydrate-binding specificity of two Xenopus proto-type galectins by site-directed mutagenesis
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
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- 巻
- 1869
- 号
- 10
- 開始ページ
- 140684
- 終了ページ
- 140684
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/j.bbapap.2021.140684
- 出版者・発行元
- Elsevier BV
The galectin family is a representative soluble lectin group, which is responsible for the modulation of various cell functions. Although the carbohydrate-binding specificity of galectins has been well-studied, the relationship between protein structure and specificity remains to be elucidated. We previously reported the characteristics of a Xenopus laevis skin galectin, xgalectin-Va, which had diverged from galectin-1. The carbohydrate selectivity of xgalectin-Va was different from that of human galectin-1 and xgalectin-Ib (a Xenopus laevis galectin-1 homolog). In this study, we clarified the key residues for this selectivity by site-directed mutagenesis. Substitution of two amino acids of xgalectin-Va, Val56Gly/Lys76Arg, greatly enhanced the binding ability to N-acetyllactosamine and conferred significant T-cell growth inhibition activity, although the wild type had no activity. These two residues, Gly54 and Arg74 in galectin-1, would cooperatively contribute to the N-acetyllactosamine recognition. The loop region between the S4 and S5 β-strands was involved in the binding to the TF-antigen disaccharide. The loop substitution successfully changed the carbohydrate selectivity of xgalectin-Va and xgalectin-Ib.
- リンク情報
- ID情報
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- DOI : 10.1016/j.bbapap.2021.140684
- ISSN : 1570-9639
- ORCIDのPut Code : 96237872
- PubMed ID : 34146732