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Journal ArticleDOI

Structure and activation of the C1 complex of complement: unraveling the puzzle

TLDR
A comprehensive, three-dimensional model of C1 is presented and insights into the mechanisms underlying its activation and the extraordinarily versatile recognition properties of its C1q subunit are provided.
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This article is published in Trends in Immunology.The article was published on 2004-07-01. It has received 230 citations till now. The article focuses on the topics: Classical complement pathway & Structural biology.

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Citations
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Journal ArticleDOI

Complement: a key system for immune surveillance and homeostasis

TL;DR: An updated view of the function, structure and dynamics of the complement network is described, its interconnection with immunity at large and with other endogenous pathways is highlighted, and its multiple roles in homeostasis and disease are illustrated.
Journal ArticleDOI

Complement System Part I - Molecular Mechanisms of Activation and Regulation

TL;DR: This article will review the mechanisms of activation of alternative, classical, and lectin pathways, the formation of C3 and C5 convertases, the action of anaphylatoxins, and the membrane-attack-complex, and discuss the importance of structure–function relationships.
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Complement System Part II: Role in Immunity.

TL;DR: Recent advances in the understanding of the role of complement in physiology and pathology are discussed, showing that complement contributes to a large variety of conditions, far exceeding the classical examples of diseases associated with complement deficiencies.
Journal ArticleDOI

C1q and tumor necrosis factor superfamily: modularity and versatility.

TL;DR: This review is an attempt to draw structural and functional parallels between the members of the C1q and TNF superfamily, which are involved in processes as diverse as host defense, inflammation, apoptosis, autoimmunity, cell differentiation, organogenesis, hibernation and insulin-resistant obesity.
References
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Journal ArticleDOI

Crystal structure of a neutralizing human IGG against HIV-1: a template for vaccine design.

TL;DR: The crystal structure at 2.7 angstrom resolution of the human antibody IgG1 b12 provides a rationale for the extensive cross-reactivity of b12 and a valuable framework for the design of HIV-1 vaccines capable of eliciting b12-like activity.
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Complement activation by beta-amyloid in Alzheimer disease

TL;DR: Direct in vitro evidence that beta-AP can bind and activate the classical complement cytolytic pathway in the absence of antibody and indirect in situ evidence that such actions occur in the AD brain in association with areas of AD pathology are provided.
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The physiological structure of human C-reactive protein and its complex with phosphocholine.

TL;DR: The structure shows how large ligands containing PC may be bound by CRP via a phosphate oxygen that projects away from the surface of the protein, inviting the design of inhibitors of CRP binding that may have therapeutic relevance to the possible role ofCRP in atherothrombotic events.
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Mapping of the C1q Binding Site on Rituxan, a Chimeric Antibody with a Human IgG1 Fc

TL;DR: The results demonstrate that the previously described C1q binding motif in murine IgG2b constituting residues E318, K320, and K322 is not applicable to a human IgG1 when challenged with either human, rabbit, or guinea pig complement and suggest that there are species-specific differences in the C 1q binding site of Igs.
Journal ArticleDOI

C1q: structure, function, and receptors.

TL;DR: The recently described crystal structure of Acrp-30, which is a serum protein secreted from adipocytes, has revealed a new C1q/TNF superfamily of proteins, which may have diverse functions, and there may be a common theme in their phylogeny and modular organisation of their distinctive globular domains.
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