1ODA
N-terminal of Sialoadhesin in complex with Me-a-9-N-(biphenyl-4-carbonyl)-amino-9-deoxy-Neu5Ac (BIP compound)
Summary for 1ODA
| Entry DOI | 10.2210/pdb1oda/pdb |
| Related | 1OD7 1OD9 1QFO 1QFP |
| Descriptor | SIALOADHESIN, ME-A-9-N-(BIPHENYL-4-CARBONYL)-AMINO-9-DEOXY-NEU5AC (2 entities in total) |
| Functional Keywords | lectin/immune system, immune system, immunoglobulin superfamily, carbohydrate binding, siglec, inhibitor design, cell adhesion, lectin-immune system complex |
| Biological source | MUS MUSCULUS (MOUSE) |
| Cellular location | Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Secreted. Isoform 3: Secreted: Q62230 |
| Total number of polymer chains | 1 |
| Total formula weight | 13821.62 |
| 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: 2003-08-14, Last modification date: 2023-12-13) |
| 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 Cited by 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: 12737821DOI: 10.1016/S0969-2126(03)00073-X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.31 Å) |
Structure validation
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