6H03

OPEN CONFORMATION OF THE MEMBRANE ATTACK COMPLEX

これはPDB形式変換不可エントリーです。

6H03 の概要

• エントリーDOI: 10.2210/pdb6h03/pdb
• 関連するPDBエントリー: 6H04
• EMDBエントリー: 0106 0107 0109 0110 0111 0112 0113
• 分子名称: Complement C5,Complement C5, 2-acetamido-2-deoxy-beta-D-glucopyranose, Complement component C8 beta chain, ... (10 entities in total)
• 機能のキーワード: c5b9, immune system
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 1631064.09

構造登録者

Menny, A.,Serna, M.,Boyd, C.M.,Gardner, S.,Joseph, A.P.,Topf, M.,Bubeck, D. (登録日: 2018-07-06, 公開日: 2018-12-19, 最終更新日: 2024-11-13)

主引用文献

Menny, A.,Serna, M.,Boyd, C.M.,Gardner, S.,Joseph, A.P.,Morgan, B.P.,Topf, M.,Brooks, N.J.,Bubeck, D.
CryoEM reveals how the complement membrane attack complex ruptures lipid bilayers.
Nat Commun, 9:5316-5316, 2018

PubMed Abstract: The membrane attack complex (MAC) is one of the immune system's first responders. Complement proteins assemble on target membranes to form pores that lyse pathogens and impact tissue homeostasis of self-cells. How MAC disrupts the membrane barrier remains unclear. Here we use electron cryo-microscopy and flicker spectroscopy to show that MAC interacts with lipid bilayers in two distinct ways. Whereas C6 and C7 associate with the outer leaflet and reduce the energy for membrane bending, C8 and C9 traverse the bilayer increasing membrane rigidity. CryoEM reconstructions reveal plasticity of the MAC pore and demonstrate how C5b6 acts as a platform, directing assembly of a giant β-barrel whose structure is supported by a glycan scaffold. Our work provides a structural basis for understanding how β-pore forming proteins breach the membrane and reveals a mechanism for how MAC kills pathogens and regulates cell functions.

PubMed: 30552328
DOI: 10.1038/s41467-018-07653-5

実験手法

ELECTRON MICROSCOPY (5.6 Å)