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


Thompson, D., Pepys, M.B., Tickle, I. and Wood, S. (2002) The Structures of Crystalline Complexes of Human Serum Amyloid P Component with Its Carbohydrate Ligand, The Cyclic Pyruvate Acetal of Galactose Journal of Molecular Biology, 320, (5), pp. 1081-1086. (doi:10.1016/S0022-2836(02)00514-4).

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Description/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.

Item Type: Article
Digital Object Identifier (DOI): doi:10.1016/S0022-2836(02)00514-4
ISSNs: 0022-2836 (print)
Subjects:
ePrint ID: 35625
Date :
Date Event
25 January 2002Submitted
26 July 2002Published
Date Deposited: 22 May 2006
Last Modified: 16 Apr 2017 22:08
Further Information:Google Scholar
URI: http://eprints.soton.ac.uk/id/eprint/35625

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