Human C-Reactive protein
The C-reactive protein is highlighted
Function
Human C-reactive protein is a member of the pentaxin family. It is involved in several host defense related functions based on its ability to recognize foreign pathogens and damaged cells of the host and to initiate their elimination by interacting with humoral and cellular effector systems in the blood. Consequently, the level of this protein in plasma increases greatly during acute phase response to tissue injury, infection, or other inflammatory stimuli."[1]
Structure
CRP consists of five identical, noncovalently associated ∼23-kDa protomers arranged symmetrically around a central pore. The term “pentraxins” has been used to describe the family of related proteins with this structure. Each protomer has been found by x-ray crystallography to be folded into two antiparallel β sheets with a flattened jellyroll topology. Each protomer has a recognition face with a phosphocholine binding site consisting of two coordinated calcium ions adjacent to a hydrophobic pocket. [2]
One of the protomers of pentaxin
Phosphocholine
Phosphocholine serves a binding target for C-reactive protein. Phosphocholines are highlighted
Function
General Function: Low-density lipoprotein particle receptor binding
Specific Function: Displays several functions associated with host defense: it promotes agglutination, bacterial capsular swelling, phagocytosis and complement fixation through its calcium-dependent binding to phosphorylcholine. Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells.[3]
Properties
Molecular Weight: 184.152 g/mol
Biofluid Locations: blood, breast milk, cerebrospinal fluid, saliva, urine
Tissue Locations: Brain, Epidermis, Fibroblasts, Intestine, Kidney, Liver, Placenta, Platelet, Stratum Corneum
Cellular location: cytoplasm, exosomes
Target: CRP [4]
