A staggered decameric assembly of human C-reactive protein stabilized by zinc ions revealed by X-ray crystallography

Human c-reactive protein (crp) is an acute phase protein,which harbours both host defence and scavenging properties. in this study,we obtained two new crystal forms of crp,where crp forms a symmetric,staggered dimer of pentamers. in one of these structures,obtained in the presence of hiv-1 tat protein,this dimer of pentamers is stabilized by two zinc ions trapped within a cleft of the effector face of crp. these two decameric interfaces involve complementary surfaces of crp pentamers and bury a large area of ∼2000 å2 per pentamer,suggesting a biological role of this interface. these two novel decameric interfaces and the involvement of zinc might have important consequences in the understanding of crp biological functions. © 2015 bentham science publishers.