1URL

N-TERMINAL DOMAIN OF SIALOADHESIN (MOUSE) IN COMPLEX WITH GLYCOPEPTIDE

Summary for 1URL

• Entry DOI: 10.2210/pdb1url/pdb
• Related: 1OD7 1OD9 1ODA 1QFO 1QFP
• Descriptor: SIALOADHESIN, ALA-GLY-HIS-THR-TRP-GLY-HIA, N-acetyl-alpha-neuraminic acid, ... (4 entities in total)
• Functional Keywords: lectin/ig-domain, sialoadhesin, oligosaccharide mimics, molecular mimicry, cell adhesion, lectin, immunoglobulin domain, sugar binding protein immune system complex, sugar binding protein, immune system, sugar binding protein-immune system complex, sugar binding protein/immune system
• Biological source: MUS MUSCULUS (MOUSE); More
• Total number of polymer chains: 2
• Total formula weight: 14278.10

Authors

Bukrinsky, J.T.,Hilaire, P.M.S.,Meldal, M.,Crocker, P.R.,Henriksen, A. (deposition date: 2003-10-31, release date: 2004-10-20, Last modification date: 2023-12-13)

Primary citation

Bukrinsky, J.T.,Hilaire, P.M.S.,Meldal, M.,Crocker, P.R.,Henriksen, A.
Complex of Sialoadhesin with a Glycopeptide Ligand
Biochim.Biophys.Acta, 1702:173-, 2004

PubMed Abstract: 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.

PubMed: 15488769
DOI: 10.1016/J.BBAPAP.2004.08.015

Experimental method

X-RAY DIFFRACTION (2.4 Å)