Structural basis of soluble membrane attack complex packaging for clearance

Anaïs Menny; Marie V. Lukassen; Emma C. Couves; Vojtech Franc; Albert J. R. Heck; Doryen Bubeck

doi:10.1038/s41467-021-26366-w

Nature Communications (Oct 2021)

Structural basis of soluble membrane attack complex packaging for clearance

Anaïs Menny,
Marie V. Lukassen,
Emma C. Couves,
Vojtech Franc,
Albert J. R. Heck,
Doryen Bubeck

Affiliations

Anaïs Menny: Department of Life Sciences, Sir Ernst Chain Building, Imperial College London
Marie V. Lukassen: Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University
Emma C. Couves: Department of Life Sciences, Sir Ernst Chain Building, Imperial College London
Vojtech Franc: Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University
Albert J. R. Heck: Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University
Doryen Bubeck: Department of Life Sciences, Sir Ernst Chain Building, Imperial College London

DOI: https://doi.org/10.1038/s41467-021-26366-w
Journal volume & issue: Vol. 12, no. 1
pp. 1 – 11

Abstract

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To prevent unregulated complement activation, extracellular chaperones capture soluble precursors to the membrane attack complex (sMAC). Here, structural analysis of sMAC reveals how clusterin recognizes heterogeneous sMAC complexes and inhibits polymerization of complement protein C9.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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