Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2023 Feb 16;14:890. doi: 10.1038/s41467-023-36441-z

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2023

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

Fig. 6 — A MAC assembles on cholesterol-rich microdomains (red hexagons) in the plasma membrane. While C7 anchors the growing MAC, C8β thins the bilayer and primes the membrane for rupture by C8α (pink). C9 joins the assembly, undergoing discrete structural transitions to form the pore. The MACPF domain of soluble C9 makes an initial contact and aligns the central β-sheet. The pore-forming β-hairpins extend sequentially. TMH1 is followed by TMH2, which allow C9 polymerization to complete the MAC pore. B CD59 is a GPI-anchored cell surface receptor that clusters in cholesterol-rich microdomains. Upon complement activation, CD59 could respond to membrane thinning by C8β and capture C8α as its transmembrane β-hairpins are extending (pink). While bound to C8α, CD59 is positioned to deflect the cascading C9 β-hairpins and divert their membrane trajectory (green). The next C9 molecule (yellow) is able to bind but trapped in an intermediate conformation in which TMH2 remains helical (red) and in which C9 polymerization is halted.