This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1oda
From Proteopedia
|
N-TERMINAL OF SIALOADHESIN IN COMPLEX WITH ME-A-9-N-(BIPHENYL-4-CARBONYL)-AMINO-9-DEOXY-NEU5AC (BIP COMPOUND)
Overview
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, ... [(full description)]
About this Structure
1ODA is a [Single protein] structure of sequence from [Mus musculus] with BDU as [ligand]. Structure known Active Site: BDU. Full crystallographic information is available from [OCA].
Reference
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
Page seeded by OCA on Tue Oct 30 15:50:24 2007
