1od9
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N-TERMINAL OF SIALOADHESIN IN COMPLEX WITH ME-A-9-N-BENZOYL-AMINO-9-DEOXY-NEU5AC (BENZ COMPOUND)
OverviewOverview
The Siglec family of receptors mediates cell surface interactions through, recognition of sialylated glycoconjugates. The crystal structure of the, N-terminal immunoglobulin-like domain of the Siglec sialoadhesin (SnD1) in, complex with 2,3-sialyllactose has informed the design of sialic acid, analogs (sialosides) that bind Siglecs with significantly enhanced, affinities and specificities. Binding assays against sialoadhesin (Sn;, Siglec-1), CD22 (Siglec-2), and MAG (Siglec-4) show a 10- to 300-fold, reduction in IC(50) values (relative to methyl-alpha-Neu5Ac) for three, sialosides bearing aromatic group modifications of the glycerol side, chain: Me-alpha-9-N-benzoyl-amino-9-deoxy-Neu5Ac (BENZ), Me-alpha-9-N-(naphthyl-2-carbonyl)-amino-9-deoxy-Neu5Ac (NAP), and, Me-alpha-9-N-(biphenyl-4-carbonyl)-amino-9-deoxy-Neu5Ac (BIP). Crystal, structures of these sialosides in complex with SnD1 suggest explanations, for the differences in specificity and affinity, providing further ideas, for compound design of physiological and potentially therapeutic, relevance.
About this StructureAbout this Structure
1OD9 is a Single protein structure of sequence from Mus musculus with SO4 and BND as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Structure-guided design of sialic acid-based Siglec inhibitors and crystallographic analysis in complex with sialoadhesin., Zaccai NR, Maenaka K, Maenaka T, Crocker PR, Brossmer R, Kelm S, Jones EY, Structure. 2003 May;11(5):557-67. PMID:12737821
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