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Structural and thermodynamic analyses reveal critical features of glycopeptide recognition by the human PILRα immune cell receptor
https://doi.org/10.24517/00067081
https://doi.org/10.24517/00067081766fe132-c0cf-4055-9f51-93d970fd6710
名前 / ファイル | ライセンス | アクション |
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PH-PR-FURUKAWA-A-51-21128.pdf (1.9 MB)
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2022-09-12 | |||||
タイトル | ||||||
タイトル | Structural and thermodynamic analyses reveal critical features of glycopeptide recognition by the human PILRα immune cell receptor | |||||
言語 | ||||||
言語 | eng | |||||
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資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
資源タイプ | journal article | |||||
ID登録 | ||||||
ID登録 | 10.24517/00067081 | |||||
ID登録タイプ | JaLC | |||||
著者 |
Furukawa, Atsushi
× Furukawa, Atsushi× Kakita, Kosuke× Yamada, Tomoki× Ishizuka, Mikihiro× Sakamoto, Jiro× Hatori, Nanao× Maeda, Naoyoshi× Ohsaka, Fumina× Saitoh, Takashi× Nomura, Takahiro× Kuroki, Kimiko× Nambu, Hisanori× Arase, Hisashi× Matsunaga, Shigeki× Anada, Masahiro× Ose, Toyoyuki× Hashimoto, Shunichi× Maenaka, Katsumi |
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著者別表示 |
古川, 敦
× 古川, 敦 |
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提供者所属 | ||||||
内容記述タイプ | Other | |||||
内容記述 | 金沢大学医薬保健研究域薬学系 | |||||
書誌情報 |
Journal of Biological Chemistry 巻 292, 号 51, p. 21128-21136, 発行日 2017-12-22 |
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ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 0021-9258 | |||||
ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 1083-351X | |||||
NCID | ||||||
収録物識別子タイプ | NCID | |||||
収録物識別子 | AA00251083 | |||||
DOI | ||||||
関連タイプ | isIdenticalTo | |||||
識別子タイプ | DOI | |||||
関連識別子 | 10.1074/jbc.M117.799239 | |||||
出版者 | ||||||
出版者 | American Society for Biochemistry and Molecular Biology Inc. | |||||
抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | Before entering host cells, herpes simplex virus-1 uses its envelope glycoprotein B to bind paired immunoglobulin-like type 2 receptor α (PILRα) on immune cells. PILRα belongs to the Siglec (sialic acid (SA)-binding immunoglobulin-like lectin)- like family, members of which bind SA. PILRα is the only Siglec member to recognize not only the sialylated O-linked sugar T antigen (sTn) but also its attached peptide region. We previously determined the crystal structure of PILRα complexed with the sTn-linked glycopeptide of glycoprotein B, revealing the simultaneous recognition of sTn and peptide by the receptor. However, the contribution of each glycopeptide component to PILRα binding was largely unclear. Here, we chemically synthesized glycopeptide derivatives and determined the thermodynamic parameters of their interaction with PILRα. We show that glycopeptides with different sugar units linking SA and peptides (i.e. "GlcNAc-Type" and "deoxy- GlcNAc-Type" glycopeptides) have lower affinity and more enthalpy-driven binding than the wild type (i.e. GalNAc-Type glycopeptide). The crystal structures of PILRα complexed with these glycopeptides highlighted the importance of stereochemical positioning of the O4 atom of the sugar moiety. These results provide insights both for understanding the unique O-glycosylated peptide recognition by the PILRα and for the rational design of herpes simplex virus-1 entry inhibitors. © 2017 by The American Society for Biochemistry and Molecular Biology, Inc. | |||||
権利 | ||||||
権利情報 | Copyright © 2017 Yamazaki et al. Published under exclusive license by The American Society for Biochemistry and Molecular Biology, Inc. | |||||
権利 | ||||||
権利情報 | This is an Open Access article under the CC BY license. | |||||
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出版タイプ | VoR | |||||
出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |||||
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識別子タイプ | URI | |||||
関連識別子 | https://www.sciencedirect.com/science/article/pii/S0021925820327617?via%3Dihub | |||||
関連名称 | https://www.sciencedirect.com/science/article/pii/S0021925820327617?via%3Dihub | |||||
関連URI | ||||||
識別子タイプ | URI | |||||
関連識別子 | https://www.journals.elsevier.com/journal-of-biological-chemistry | |||||
関連名称 | https://www.journals.elsevier.com/journal-of-biological-chemistry | |||||
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識別子タイプ | URI | |||||
関連識別子 | http://www.asbmb.org/ | |||||
関連名称 | http://www.asbmb.org/ |