C-Reactive Protein (CRP) Sequences
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Introduction
C-reactive protein (CRP) is an acute protein that rises sharply in the plasma when the body is infected or damaged by tissue. CRP sequence is a typical pentameric family of proteins whose crystal structures were resolved by X-Ray technology in 1999 and 1996, respectively. CRP sequences are composed of five identical subunits arranged in a five-symmetric mode with a hole formed in the middle. The outer diameter of the pentamer is 10.2 nm. The diameter of middle hole is 3 nm. The diameter single subunit is 3.6 nm. Each subunit of CRP sequence is folded from 206 amino acids into two inverted β-sheets. The two sides of this pentameric ring structure. One is called the effect surface, which is the junction of the C1q and Fcγ receptors. The other side is the recognition surface, which is the PC binding surface. At the binding site of PC, there are two calcium ion binding sites. Binding of PC is also calcium ion dependent. There are three main salt bridges at the adjacent positions of each subunit, 115-123, 40-42, 197-202.
Mechanism of action
When the body is infected or damaged by tissue, CRP can activate complement and enhance the phagocytosis of phagocytic cells, which plays a conditioning role. This can remove pathogenic microorganisms and damaged, necrotic, and apoptotic tissue cells. CRP recognizes foreign substances and activates the complement system. CRP can enhance the conditioning effect and enhance the phagocytosis of phagocytic cells. CRP binds to platelet activating factor and reduces inflammation. CRP binds to chromosomes and eliminates cellular DNA in necrotic tissue.
Application of C-reactive protein (CRP)
One of the important markers in the clinical diagnosis of infectious diseases is C-reactive protein. Clinical combination of C-reactive protein and blood routine indicators can further improve the diagnosis and treatment of the disease. In addition, the level of CRP can predict the occurrence of cardiovascular disease. As a clinical test, CRP has the advantages of cheap detection and popularization.
Reference
- Darren, T., Mark, B. P., Steve, P. W. (1999). The physiological structure of human C-reactive protein and its complex with phosphocholine. Structure, 7(2), 169-177.
