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The C-reactive protein has been given this name because it precipitates the C polysaccharide in the cell wall.[3]
Structure
CRP structure
Ser53, His95, Cys97, Asp112, Gly113, Gly136, Gly154, Val165, Leu166, Ile171, and Gly196 are the highly conserved residues in the primary sequence of CRP.[3]
The C-reactive protein is a homopentamer of non-covalently bound subunits. Each subunit is a 25 Da protein consisting of 224 residues bound together. The secondary structure is formed of four α-helices and three β-sheets (five-stranded, three-stranded and seven-stranded).[4] The predominant structure is β-sheet [5] but short helical regions can be notice for residues 43 and 185.[3] Residues Glu197 and Lys123 in CRP form an intermolecular ion pair.[6]
Calcium binding-site
CRP is a calcium dependent strcuture. Effectively, Ca2+ is required for PC binding, and more precisely for the formation of the PCbinding site. Structural rearrangements of the CRP occur when the protein binds calcium. The protection against denaturation and proteolysis. [7]
PC binding site
PC stands for phosphocoline. It is a phospholipid in cell membranes and a plasma lipoproteins.[6] Phe-66 and Glu-81 are the two key residues that enable the binding of PC. [3]
Function
Biomedical interest
Healthy humans have CRP rate which is generally about 1 μg/mL.[3] CRP level is 1000 times higher in a cytokine-mediated response due to tissue injury, infection and inflammation. Therefore the CRP rate in serum is common use to detect the activity of a disease.[6] CRP can be defined as a target for the development of cardioprotection and neuroprotection.[3]
Structural highlights
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