7WZ8

Structure of human langerin complex in Birbeck granules

これはPDB形式変換不可エントリーです。

7WZ8 の概要

• エントリーDOI: 10.2210/pdb7wz8/pdb
• EMDBエントリー: 32906
• 分子名称: SNAP-tag,C-type lectin domain family 4 member K (1 entity in total)
• 機能のキーワード: birbeck granule, c-type lectin, langerhans cell, virus defense, membrane protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 363286.64

構造登録者

Oda, T.,Yanagisawa, H. (登録日: 2022-02-17, 公開日: 2022-06-22, 最終更新日: 2024-10-23)

主引用文献

Oda, T.,Yanagisawa, H.,Shinmori, H.,Ogawa, Y.,Kawamura, T.
Cryo-electron tomography of Birbeck granules reveals the molecular mechanism of langerin lattice formation.
Elife, 11:e79990-e79990, 2022

PubMed Abstract: Langerhans cells are specialized antigen-presenting cells localized within the epidermis and mucosal epithelium. Upon contact with Langerhans cells, pathogens are captured by the C-type lectin langerin and internalized into a structurally unique vesicle known as a Birbeck granule. Although the immunological role of Langerhans cells and Birbeck granules have been extensively studied, the mechanism by which the characteristic zippered membrane structure of Birbeck granules is formed remains elusive. In this study, we observed isolated Birbeck granules using cryo-electron tomography and reconstructed the 3D structure of the repeating unit of the honeycomb lattice of langerin at 6.4 Å resolution. We found that the interaction between the two langerin trimers was mediated by docking the flexible loop at residues 258-263 into the secondary carbohydrate-binding cleft. Mutations within the loop inhibited Birbeck granule formation and the internalization of HIV pseudovirus. These findings suggest a molecular mechanism for membrane zippering during Birbeck granule biogenesis and provide insight into the role of langerin in the defense against viral infection.

PubMed: 35758632
DOI: 10.7554/eLife.79990

実験手法

ELECTRON MICROSCOPY (6.4 Å)