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CRP binds to phosphocholine which is exposed on died or dying cells and expressed on the surfaces of pathogens. Then, it may activate the complement system via interaction with C1q, and enhance phagocytosis by macrophages via its binding to Fcγ receptors. In addition to the fact that this protein has been highly conserved during evolution, this suggests that CRP is a very important part of the innate immune response, in the host defense. | CRP binds to phosphocholine which is exposed on died or dying cells and expressed on the surfaces of pathogens. Then, it may activate the complement system via interaction with C1q, and enhance phagocytosis by macrophages via its binding to Fcγ receptors. In addition to the fact that this protein has been highly conserved during evolution, this suggests that CRP is a very important part of the innate immune response, in the host defense. | ||
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| + | This feature of amount increasing is curently used as a marker of inflammation in patients. | ||
CRP belong to the pentraxin family. | CRP belong to the pentraxin family. | ||
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Human C-reactive protein (CRP)
The C-reactive protein (CRP) is a plasma protein, mainly synthesized by the liver. Its concentration may increase rapidly, as much as 1000-fold or more, in response to tissue injury, infection and inflammation: It's an acute-phase protein.
CRP binds to phosphocholine which is exposed on died or dying cells and expressed on the surfaces of pathogens. Then, it may activate the complement system via interaction with C1q, and enhance phagocytosis by macrophages via its binding to Fcγ receptors. In addition to the fact that this protein has been highly conserved during evolution, this suggests that CRP is a very important part of the innate immune response, in the host defense.
This feature of amount increasing is curently used as a marker of inflammation in patients.
CRP belong to the pentraxin family.
Structure of CRP
CRP is a pentamer: it contains five identical 23-kDa protomers, noncovalently associated (van der Waals contacts or hydrogen bonding) around a central pore. All members of the “pentraxins” family have this general structure.
Each protomer has a recognition face (also called face B) with a phosphocholine binding site (carrying two calcium ions), made of a two-layered β sheet. The other face - the effector face (or face A) - where complement C1q and Fc receptors bind, contain a single α helix. Consequently, the pentamer consist of five α helices on one side, and ten calcium ions on the other.
