Abstract
The three-dimensional structure of pentameric human serum amyloid P component at high resolution, the first reported for a pentraxin, reveals that the tertiary fold is remarkably similar to that of the legume lectins. Carboxylate and phosphate compounds bind directly to two calcium ions; interactions with a carboxyethylidene ring are mediated by Asn 59 and Gin 148 ligands of the calcium ions. These X-ray results indicate the probable modes of binding of the biologically important ligands, DNA and amyloid fibrils.
Original language | English |
---|---|
Pages (from-to) | 338-345 |
Journal | Nature |
Volume | 367 |
Issue number | 6461 |
DOIs | |
Publication status | Published - 27 Jan 1994 |