3-DIMENSIONAL STRUCTURE OF HUMAN C-REACTIVE PROTEIN

The structure of the classical acute phase reactant human C-reactive p rotein provides evidence that phosphocholine binding is mediated throu gh calcium and a hydrophobic pocket centred on Phe 66. The residue Glu 81 is suitably positioned to interact with the choline group. A cleft on the pentameric face opposite to that containing the calcium site m ay have an important functional role. The structure provides insights into the molecular mechanisms by which this highly conserved plasma pr otein, for which no polymorphism or deficiency state is known, may exe rt its biological role.