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Structural Basis for the Function; Complement Component C4 within the Classical and Lectin Pathways; Complement
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DOI：10.4049/jimmunol.1500087.png)
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摘要
En 中文
Complement component C4 is a central protein in the classical and lectin pathways within the complement system. During activation;
complement, its major fragment C4b becomes covalently attached to the surface;
pathogens and altered selftissue, where it acts as an opsonin marking the surface for removal. Moreover, C4b provides a platform for assembly;
the proteolytically active convertases that mediate downstream complement activation by cleavage;
C3 and C5. In this article, we present the crystal and solution structures;
the 195-kDa C4b. Our results provide the molecular details;
the rearrangement accompanying C4 cleavage and suggest intramolecular flexibility;
C4b. The conformations;
C4b and its paralogue C3b are shown to be remarkably conserved, suggesting that the convertases from the classical and alternative pathways are likely to share their overall architecture and mode;
substrate recognition. We propose an overall molecular model for the classical pathway C5 convertase in complex with C5, suggesting that C3b increases the affinity for the substrate by inducing conformational changes in C4b rather than a direct interaction with C5. C4b-specific features revealed by our structural studies are probably involved in the assembly;
the classical pathway C3/C5 convertases and C4b binding to regulators.
Keyword:
4TH COMPONENT
CONFORMATIONAL-CHANGES
C4B-BINDING PROTEIN
COVALENT BINDING
C5 CONVERTASE
AMINO-ACIDS
BETA-CHAIN
FACTOR-H
C3B
ACTIVATION
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期刊
IF:
3.4
论文数:
3.7W
被引数:
9.9W
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引用论文
Structure of complement fragment C3b-factor H and implications for host protection by complement regulators.png)
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