- C1q is a 460-kDa protein with the overall shape of a bouquet of flowers, comprising six heterotrimeric collagen-like triple helices that associate in their N-terminal half to form a “stalk,” then diverge to form individual “stems”, each terminating in a C-terminal heterotrimeric globular domain (4).www.jbc.org/article/S0021-9258(20)75985-5/fulltext
Structural and functional anatomy of the globular …
The globular head is believed to be involved in the binding viral envelope proteins, e.g. C1q binds to the envelope protein p15e of Type C retroviruses leading to the classical pathway mediated lysis of the virus.
The Crystal Structure of the Globular Head of …
We report here the x-ray structure of the heterotrimeric globular head of C1q, the domain responsible for the versatile recognition properties of this protein.
- Author: Christine Gaboriaud, Jordi Juanhuix, Arnaud Gruez, Monique Lacroix, Claudine Darnault, David Pignol,...
- Publish Year: 2003
Complement Component C1q: Historical Perspective of …
Primary targets for the six globular heads of C1q are the multiple Fc regions presented within immune complexes, containing IgG or IgM antibodies. Well-defined non-immunoglobulin targets, for the C1q heads, include CRP and …
Complement Component 1q (C1q) - Sino Biological
Complement component C1q is a calcium-dependent sugar-binding protein, a lectin, belonging to the collectin family of proteins, which contains both collagen-like and lectin domains hence the …
C1q: A fresh look upon an old molecule - PMC - PubMed Central …
C1q is a complex glycoprotein assembled from 18 polypeptide chains, with a C-terminal globular head region that mediates recognition of diverse molecular structures, and an N-terminal …
Frontiers | Complement Component C1q: Historical Perspective of …
Apr 10, 2018 · The globular heads of C1q are similar to domains found within the tumor necrosis factor (TNF) superfamily of proteins, and have been shown to bind to a very wide range of …
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C1q: Its Functions within the Innate and Adaptive Immune …
Jul 1, 2005 · C1q is activated by the binding of its globular head domain to the Fc region of aggregated IgG and IgM molecules in immune complexes. Thus, in its role as the recognition …
- Author: Richard D. Sontheimer, Emil Racila, Doina M. Racila
- Publish Year: 2005
1PK6: Globular Head of the Complement System …
Jun 5, 2003 · Plausible three-dimensional models of the C1q globular domain in complex with two of its physiological ligands, C-reactive protein and IgG, are proposed, highlighting two of the possible recognition modes of C1q.
Modular Organization of the Carboxyl-Terminal, Globular Head …
Jul 15, 2003 · The first step in the activation of the classical complement pathway, by immune complexes, involves the binding of the globular heads of C1q to the Fc regions of aggregated …
RCSB PDB - 2JG9: Crystallographic structure of human C1q globular heads …
Feb 9, 2007 · C1Q Binds Phosphatidylserine and Likely Acts as a Multiligand-Bridging Molecule in Apoptotic Cell Recognition. Efficient apoptotic cell clearance is critical for maintenance of …
