Structure of the poly-C9 component of the complement membrane attack complex

The membrane attack complex is a heteromeric assembly of complement proteins where multiple copies of C9 are recruited by the C5b678 complex to form lytic pores in pathogen membranes. Here the authors present the structure of a soluble pore-like form of the C9 component that reveals details of the o...

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Autores principales:	Natalya V. Dudkina, Bradley A. Spicer, Cyril F. Reboul, Paul J. Conroy, Natalya Lukoyanova, Hans Elmlund, Ruby H. P. Law, Susan M. Ekkel, Stephanie C. Kondos, Robert J. A. Goode, Georg Ramm, James C. Whisstock, Helen R. Saibil, Michelle A. Dunstone
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/a2649e95879f4957bec6ff1711385015
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spelling	oai:doaj.org-article:a2649e95879f4957bec6ff17113850152021-12-02T17:31:34ZStructure of the poly-C9 component of the complement membrane attack complex10.1038/ncomms105882041-1723https://doaj.org/article/a2649e95879f4957bec6ff17113850152016-02-01T00:00:00Zhttps://doi.org/10.1038/ncomms10588https://doaj.org/toc/2041-1723The membrane attack complex is a heteromeric assembly of complement proteins where multiple copies of C9 are recruited by the C5b678 complex to form lytic pores in pathogen membranes. Here the authors present the structure of a soluble pore-like form of the C9 component that reveals details of the oligomerization interfaces.Natalya V. DudkinaBradley A. SpicerCyril F. ReboulPaul J. ConroyNatalya LukoyanovaHans ElmlundRuby H. P. LawSusan M. EkkelStephanie C. KondosRobert J. A. GoodeGeorg RammJames C. WhisstockHelen R. SaibilMichelle A. DunstoneNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-6 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Natalya V. Dudkina Bradley A. Spicer Cyril F. Reboul Paul J. Conroy Natalya Lukoyanova Hans Elmlund Ruby H. P. Law Susan M. Ekkel Stephanie C. Kondos Robert J. A. Goode Georg Ramm James C. Whisstock Helen R. Saibil Michelle A. Dunstone Structure of the poly-C9 component of the complement membrane attack complex
description	The membrane attack complex is a heteromeric assembly of complement proteins where multiple copies of C9 are recruited by the C5b678 complex to form lytic pores in pathogen membranes. Here the authors present the structure of a soluble pore-like form of the C9 component that reveals details of the oligomerization interfaces.
format	article
author	Natalya V. Dudkina Bradley A. Spicer Cyril F. Reboul Paul J. Conroy Natalya Lukoyanova Hans Elmlund Ruby H. P. Law Susan M. Ekkel Stephanie C. Kondos Robert J. A. Goode Georg Ramm James C. Whisstock Helen R. Saibil Michelle A. Dunstone
author_facet	Natalya V. Dudkina Bradley A. Spicer Cyril F. Reboul Paul J. Conroy Natalya Lukoyanova Hans Elmlund Ruby H. P. Law Susan M. Ekkel Stephanie C. Kondos Robert J. A. Goode Georg Ramm James C. Whisstock Helen R. Saibil Michelle A. Dunstone
author_sort	Natalya V. Dudkina
title	Structure of the poly-C9 component of the complement membrane attack complex
title_short	Structure of the poly-C9 component of the complement membrane attack complex
title_full	Structure of the poly-C9 component of the complement membrane attack complex
title_fullStr	Structure of the poly-C9 component of the complement membrane attack complex
title_full_unstemmed	Structure of the poly-C9 component of the complement membrane attack complex
title_sort	structure of the poly-c9 component of the complement membrane attack complex
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/a2649e95879f4957bec6ff1711385015
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Structure of the poly-C9 component of the complement membrane attack complex

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