HUSCAP logo Hokkaido Univ. logo

Hokkaido University Collection of Scholarly and Academic Papers >
Faculty of Pharmaceutical Sciences >
Peer-reviewed Journal Articles, etc >

Structural analysis for glycolipid recognition by the C-type lectins Mincle and MCL

Files in This Item:
WoS_63102_Furukarwa-Mincle-MCL_KU47.pdf本文2.09 MBPDFView/Open
WoS_63102_Furukarwa-Mincle-MCL_sup16.pdfSupporting Information861.86 kBPDFView/Open
Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/56593

Title: Structural analysis for glycolipid recognition by the C-type lectins Mincle and MCL
Authors: Furukawa, Atsushi Browse this author
Kamishikiryo, Jun Browse this author
Mori, Daiki Browse this author
Toyonaga, Kenji Browse this author
Okabe, Yuki Browse this author
Toji, Aya Browse this author
Kanda, Ryo Browse this author
Miyake, Yasunobu Browse this author
Ose, Toyoyuki Browse this author →KAKEN DB
Yamasaki, Sho Browse this author →KAKEN DB
Maenaka, Katsumi Browse this author →KAKEN DB
Keywords: X-ray crystallography
innate immunity
mycobacteria
pattern-recognition receptors
myeloid cells
Issue Date: 22-Oct-2013
Publisher: Natl acad sciences
Journal Title: Proceedings of the national academy of sciences of the united states of america
Volume: 110
Issue: 43
Start Page: 17438
End Page: 17443
Publisher DOI: 10.1073/pnas.1312649110
PMID: 24101491
Abstract: Mincle [macrophage inducible Ca2+-dependent (C-type) lectin; CLEC4E] and MCL (macrophage C-type lectin; CLEC4D) are receptors for the cord factor TDM (trehalose-6,6'-dimycolate), a unique glycolipid of mycobacterial cell-surface components, and activate immune cells to confer adjuvant activity. Although it is known that receptor-TDM interactions require both sugar and lipid moieties of TDM, the mechanisms of glycolipid recognition by Mincle and MCL remain unclear. We here report the crystal structures of Mincle, MCL, and the Mincle-citric acid complex. The structures revealed that these receptors are capable of interacting with sugar in a Ca2+-dependent manner, as observed in other C-type lectins. However, Mincle and MCL uniquely possess shallow hydrophobic regions found adjacent to their putative sugar binding sites, which reasonably locate for recognition of fatty acid moieties of glycolipids. Functional studies using mutant receptors as well as glycolipid ligands support this deduced binding mode. These results give insight into the molecular mechanism of glycolipid recognition through C-type lectin receptors, which may provide clues to rational design for effective adjuvants.
Type: article (author version)
URI: http://hdl.handle.net/2115/56593
Appears in Collections:薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 古川 敦

Export metadata:

OAI-PMH ( junii2 , jpcoar )

MathJax is now OFF:


 

 - Hokkaido University