Genetic Base of C-Reactive Proteins
First identified by William Tillett and Thomas Frances in 1930, C-reactive proteins were named after a type of streptococcus pneumoniae extract the team called “Fraction C." When the disease was administered, the two scientists found that the protein would react to fight against inflammation.
The gene for CRP is located on the first chromosome, 1q23 and is comprised of two exons and one intron. The C-reactive protein is first synthesized as a 206 amino acid polypeptide, then secreted by the hepatocytes as a non-glycosylated monomer with a molar mass of 25106 daltons.
Most scientists see the C-reactive protein structure as a jellyroll structure which forms into a symmetrical unit when it is fully active.
Occasionally, sugars may attach to the CRP. Certain diseases can cause amino acids to abandon its structure. This makes the protein structure vulnerable to glycosylation from galactose, glucose, mannose or sialic acid. This changes the pattern in which the protein is structured slightly and can make the blood cells vulnerable to various parasites. The most common diseases in which this occurs are bone cancer, lupus, leukemia and tuberculosis.
Above: Computer model of C-reactive protein. (Image credit: Skolstoe at Wikimedia Commons, http://en.wikipedia.org/wiki/File:CRP_pretty.png, public domain.)