| Item type |
デフォルトアイテムタイプ_（フル）(1) |
| 公開日 |
2023-03-18 |
| タイトル |
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|
タイトル |
Structural implication for the impaired binding of W150A mutant LOX-1 to oxidized low density lipoprotein, OxLDL |
|
言語 |
en |
| 作成者 |
Nakano, Shogo
Sugihara, Mamoru
Yamada, Risato
Katayanagi, Katsuo
Tate, Shin-ichi
|
| アクセス権 |
|
|
アクセス権 |
open access |
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アクセス権URI |
http://purl.org/coar/access_right/c_abf2 |
| 権利情報 |
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|
権利情報 |
(c) 2012 Elsevier B.V. All rights reserved. |
| 主題 |
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|
主題Scheme |
Other |
|
主題 |
C-type lectin-like domain |
| 主題 |
|
|
主題Scheme |
Other |
|
主題 |
Oxidized low density lipoprotein |
| 主題 |
|
|
主題Scheme |
Other |
|
主題 |
Atherosclerosis |
| 主題 |
|
|
主題Scheme |
Other |
|
主題 |
Receptor structure |
| 主題 |
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|
主題Scheme |
Other |
|
主題 |
Pattern recognition receptor |
| 主題 |
|
|
主題Scheme |
NDC |
|
主題 |
430 |
| 内容記述 |
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|
内容記述 |
Lectin-like oxidized lipoprotein (OxLDL) receptor 1, LOX-1, is the major OxLDL receptor expressed on vascular endothelial cells. We have previously reported the ligand-recognition mode of LOX-1 based on the crystal structure of the ligand binding domain (C-type lectin-like domain, CTLD) and surface plasmon resonance analysis, which suggested that the functional significance of the CTLD dimer (the 'canonical' dimer) is to harbor the characteristic "basic spine" on its surface. In this study, we have identified the key inter-domain interactions in retaining the canonical CTLD dimer by X-ray structural analysis of the inactive mutant W150A CTLD. The canonical CTLD dimer forms through tight hydrophobic interactions, in which W150 engages in a lock-and-key manner and represents the main interaction. The loss of the Trp ring by mutation to Ala prevents the formation of the canonical dimer, as elucidated from docking calculations using the crystal structure of W150A CTLD. The results emphasize that the canonically formed CTLD dimer is essential for LOX-1 to bind to OxLDL, which supports our proposed view that the basic spine surface present in the correctly formed dimer plays a primal role in OxLDL recognition. This concept provides insight into the pathogenic pattern recognized by LOX-1 as a member of the pattern recognition receptors. |
|
言語 |
en |
| 出版者 |
|
|
出版者 |
Elsevier Science BV |
| 言語 |
|
|
言語 |
eng |
| 資源タイプ |
|
|
資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
|
資源タイプ |
journal article |
| 出版タイプ |
|
|
出版タイプ |
AO |
|
出版タイプResource |
http://purl.org/coar/version/c_b1a7d7d4d402bcce |
| 関連情報 |
|
|
|
識別子タイプ |
DOI |
|
|
関連識別子 |
10.1016/j.bbapap.2012.02.003 |
| 関連情報 |
|
|
|
識別子タイプ |
DOI |
|
|
関連識別子 |
http://dx.doi.org/10.1016/j.bbapap.2012.02.003 |
| 収録物識別子 |
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|
収録物識別子タイプ |
ISSN |
|
収録物識別子 |
1570-9639 |
| 収録物識別子 |
|
|
収録物識別子タイプ |
NCID |
|
収録物識別子 |
AA11966765 |
| 開始ページ |
|
|
開始ページ |
739 |
| 書誌情報 |
Biochimica et Biophysica Acta - Proteins and Proteomics
Biochimica et Biophysica Acta - Proteins and Proteomics
巻 1824,
号 5,
p. 739-749,
発行日 2012
|
| 旧ID |
34810 |
BBA-ProteinsProteomics_1824_739.pdf (3.7 MB)
