Thompson, D., Pepys, M.B., Tickle, I. and Wood, S.
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), . (doi:10.1016/S0022-2836(02)00514-4).
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.
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