STRUCTURE OF PENTAMERIC HUMAN SERUM AMYLOID-P COMPONENT

The three-dimensional structure of pentameric human serum amyloid P co mponent at high resolution, the first reported for a pentraxin, reveal s that the tertiary fold is remarkably similar to that of the legume l ectins. Carboxylate and phosphate compounds bind directly to two calci um ions; interactions with a carboxyethylidene ring are mediated by As n 59 and Gln 148 ligands of the calcium ions. These X-ray results indi cate the probable modes of binding of the biologically important ligan ds, DNA and amyloid fibrils.