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| [[Image:1od7.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1od7| PDB=1od7 | SCENE= }} | | {{STRUCTURE_1od7| PDB=1od7 | SCENE= }} |
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| '''N-TERMINAL OF SIALOADHESIN IN COMPLEX WITH ME-A-9-N-(NAPHTHYL-2-CARBONYL)-AMINO-9-DEOXY-NEU5AC (NAP COMPOUND)'''
| | ===N-TERMINAL OF SIALOADHESIN IN COMPLEX WITH ME-A-9-N-(NAPHTHYL-2-CARBONYL)-AMINO-9-DEOXY-NEU5AC (NAP COMPOUND)=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_12737821}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12737821 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12737821}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Inhibitor design]] | | [[Category: Inhibitor design]] |
| [[Category: Siglec]] | | [[Category: Siglec]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:41:35 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:18:56 2008'' |
