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The Structures of Crystalline Complexes of Human Serum Amyloid P Component with Its Carbohydrate Ligand, The Cyclic Pyruvate Acetal of Galactose

By D. Thompson, M.B. Pepys, I. Tickle and S. Wood

Abstract

Two monoclinic (P21) crystal forms of human serum amyloid P component (SAP) in complex with the 4,6-pyruvate acetal of b-D-galactose (MObDG) were prepared. Structure analysis by molecular replacement and refinement at 2.2 A ° resolution revealed that crystal form 1 (a 1/4 95:76 A; b 1/4 70:53 A; c 1/4 103:41 A; b 1/4 96:808) contained a pentamer in the asymmetric unit with a structure very similar to that of the published search model. The mode of ligand co-ordination was also similar except that four of the five subunits showed bound ligand with an additional H-bond between O1 of the galactose and the side-chain of Lys79. One sub-unit showed no bound ligand and a vacant calcium site close to a crystal contact. The 2.6 A ° resolution structure of crystal form 2 (a 1/4 118:60 A; b 1/4 109:10 A; c 1/4 120:80 A and b 1/4 95:168) showed ten sub-units in the asymmetric unit, all with two bound calcium ions and ligand. The most extensive protein–protein interactions between pentamers describe an AB face-to-face interaction involving 15 ion pairs that sandwiches five molecules of bound MObDG at the interface

Topics: QH301
Year: 2002
OAI identifier: oai:eprints.soton.ac.uk:35625
Provided by: e-Prints Soton
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