NDLI: Structural basis of the C1q/C1s interaction and its central role in assembly of the C1 complex of complement activation.

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Structural basis of the C1q/C1s interaction and its central role in assembly of the C1 complex of complement activation.

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Structural basis of the C1q/C1s interaction and its central role in assembly of the C1 complex of complement activation.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Gingras, Alexandre R. Gál, Péter Schwaeble, Wilhelm J. Mitchell, Daniel A. Moody, Peter C. E. Sheikh, Md Arif Wallis, Russell Marshall, Jamie E. Panchal, Roshni Venkatraman Girija, Umakhanth
Description	Author Affiliation: Venkatraman Girija U ( Department of Infection, University of Leicester, Leicester LE1 9HN, United Kingdom.);
Abstract	Complement component C1, the complex that initiates the classical pathway of complement activation, is a 790-kDa assembly formed from the target-recognition subcomponent C1q and the modular proteases C1r and C1s. The proteases are elongated tetramers that become more compact when they bind to the collagen-like domains of C1q. Here, we describe a series of structures that reveal how the subcomponents associate to form C1. A complex between C1s and a collagen-like peptide containing the C1r/C1s-binding motif of C1q shows that the collagen binds to a shallow groove via a critical lysine side chain that contacts Ca(2+)-coordinating residues. The data explain the Ca(2+)-dependent binding mechanism, which is conserved in C1r and also in mannan-binding lectin-associated serine proteases, the serine proteases of the lectin pathway activation complexes. In an accompanying structure, C1s forms a compact ring-shaped tetramer featuring a unique head-to-tail interaction at its center that replicates the likely arrangement of C1r/C1s polypeptides in the C1 complex. Additional structures reveal how C1s polypeptides are positioned to enable activation by C1r and interaction with the substrate C4 inside the cage-like assembly formed by the collagenous stems of C1q. Together with previously determined structures of C1r fragments, the results reported here provide a structural basis for understanding the early steps of complement activation via the classical pathway.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	34
Volume Number	110
Language	English
Publisher	National Academy of Sciences
Publisher Date	2013-08-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Complement Activation Immunology Complement C1 Chemistry Complement C1q Complement C1s Immunity, Innate Models, Molecular Protein Conformation Animals CHO Cells Chromatography, Affinity Chromatography, Gel Genetics Metabolism Cricetinae Cricetulus Crystallization Escherichia Coli Protein Binding Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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