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Revision as of 17:04, 30 October 2007
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N-TERMINAL DOMAIN OF SIALOADHESIN (MOUSE) IN COMPLEX WITH GLYCOPEPTIDE
OverviewOverview
Sialoadhesin is a sialic acid-binding immunoglobulin-like lectin (Siglec), expressed on subsets of macrophages. It is a model system for Siglec, receptor-mediated cell surface interactions through binding of sialylated, glycoconjugates. The N-terminal sialoadhesin domain can mediate sialic, acid-binding on its own. The structure of this domain has been determined, in complex with a sialic acid-containing heptapeptide, (Ala-Gly-His-Thr(Neu5Ac)-Trp-Gly-His). The affinity of sialoadhesin for, this ligand is four times higher than the affinity for the natural linkage, 2,3'-sialyllactose. The structure of the glycopeptide complex suggests, strategies for ligand optimization and provides possible explanations for, the observed differences in specificities among the Siglecs.
About this StructureAbout this Structure
1URL is a [Protein complex] structure of sequences from [Mus musculus] with SIA as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Complex of sialoadhesin with a glycopeptide ligand., Bukrinsky JT, St Hilaire PM, Meldal M, Crocker PR, Henriksen A, Biochim Biophys Acta. 2004 Nov 1;1702(2):173-9. PMID:15488769
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