1OD9

N-terminal of Sialoadhesin in complex with Me-a-9-N-benzoyl-amino-9-deoxy-Neu5Ac (BENZ compound)

Summary for 1OD9

• Entry DOI: 10.2210/pdb1od9/pdb
• Related: 1OD7 1ODA 1QFO 1QFP
• Descriptor: SIALOADHESIN, methyl 5-acetamido-3,5,9-trideoxy-9-[(phenylcarbonyl)amino]-D-glycero-alpha-D-galacto-non-2-ulopyranosidonic acid, SULFATE ION, ... (4 entities in total)
• Functional Keywords: lectin/immune system, immune system, immunoglobulin superfamily, carbohydrate binding, siglec, inhibitor design, lectin-immune system complex
• Biological source: MUS MUSCULUS (MOUSE)
• Total number of polymer chains: 1
• Total formula weight: 13841.59

Authors

Zaccai, N.R.,Maenaka, K.,Maenaka, T.,Crocker, P.R.,Brossmer, R.,Kelm, S.,Jones, E.Y. (deposition date: 2003-02-14, release date: 2003-05-16, Last modification date: 2024-11-20)

Primary citation

Zaccai, N.R.,Maenaka, K.,Maenaka, T.,Crocker, P.R.,Brossmer, R.,Kelm, S.,Jones, E.Y.
Structure-Guided Design of Sialic Acid-Based Siglec Inhibitors and Crystallographic Analysis in Complex with Sialoadhesin
Structure, 11:557-, 2003

PubMed Abstract: 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.

PubMed: 12737821
DOI: 10.1016/S0969-2126(03)00073-X

Experimental method

X-RAY DIFFRACTION (2.1 Å)