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Revision as of 14:04, 30 October 2007
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N-TERMINAL DOMAIN OF SIALOADHESIN (MOUSE) IN COMPLEX WITH GLYCOPEPTIDE
Overview
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 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].
Reference
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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