1url
From Proteopedia
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'''N-TERMINAL DOMAIN OF SIALOADHESIN (MOUSE) IN COMPLEX WITH GLYCOPEPTIDE''' | '''N-TERMINAL DOMAIN OF SIALOADHESIN (MOUSE) IN COMPLEX WITH GLYCOPEPTIDE''' | ||
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[[Category: Hilaire, P M.S.]] | [[Category: Hilaire, P M.S.]] | ||
[[Category: Meldal, M.]] | [[Category: Meldal, M.]] | ||
| - | [[Category: | + | [[Category: Cell adhesion]] |
| - | [[Category: | + | [[Category: Immunoglobulin domain]] |
| - | [[Category: | + | [[Category: Lectin]] |
| - | [[Category: | + | [[Category: Molecular mimicry]] |
| - | [[Category: | + | [[Category: Oligosaccharide mimic]] |
| - | [[Category: | + | [[Category: Sialoadhesin]] |
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 08:35, 3 May 2008
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. 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 Page seeded by OCA on Sat May 3 11:35:36 2008
