1od9: Difference between revisions

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.

1OD9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with SO4 and BND as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: BND. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OD9 OCA].  

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