
C3b - Wikipedia
C3b is the larger of two elements formed by the cleavage of complement component 3, and is considered an important part of the innate immune system. C3b is potent in opsonization: …
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C3b - an overview | ScienceDirect Topics
C3b is a highly unstable molecule that has a unique thioester that allows covalent binding to a microbial cell. Some C3b fragments bind to the target cell, where they act as opsonins. In the …
Complement Component C3b - an overview | ScienceDirect Topics
Complement Component C3b is a serum protein that plays a crucial role in innate and adaptive immunity by binding covalently to pathogens, acting as an opsonin to target them for …
11.3B: The Complement System - Biology LibreTexts
2023年8月31日 · One portion of the C3b binds to proteins and polysaccharides on microbial surfaces; another portion attaches to CR1 receptors on phagocytes, B-lymphocytes, and …
Complement Pathways: Types, Functions, Regulation
C3b binds the surface of foreign cells and then binds to another serum protein called factor B. Now factor B exposes the site which serves as the substrate for enzymatically active serum …
The structure of complement C3b provides insights into …
2006年10月15日 · Here we present a structure of C3b that reveals a marked loss of secondary structure in the CUB (for ‘complement C1r/C1s, Uegf, Bmp1’) domain, which together with the …
C3b - Complement Tech
C3b is central to the function of all three pathways of complement (Law, S.K.A. and Reid, K.B.M. (1995)). Initiation of each pathway generates proteolytic enzyme complexes (C3 convertases) …
C3-convertase - Wikipedia
C3b, the larger fragment, becomes covalently attached to the microbial surface or to the antibody molecules through the thioester domain at the site of complement activation. After cleavage …
Complement System - Immunology; Allergic Disorders - Merck …
The 3 activation pathways converge into a final common pathway when C3 convertase cleaves C3 into C3a and C3b (see figure Complement Activation Pathways). C3 cleavage may result …