Complex of sialoadhesin with a glycopeptide ligand

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

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.

TidsskriftBiochimica et Biophysica Acta - Proteins and Proteomics
Udgave nummer2
Sider (fra-til)173-179
Antal sider7
StatusUdgivet - 1 nov. 2004
Eksternt udgivetJa

Bibliografisk note

Funding Information:
We thank Pia Breddam for outstanding technical assistance in the protein purification step and Dr. Yngve Cerenius for beam line assistance. Dr. Koen M. Halkes is thanked for synthesis of the sialopeptide ligand. This research was supported by the Danish National Research Council (DANSYNC grant) and the Danish National Research Foundation (SPOCC center). Use of the MAXLABII synchrotron was supported by the European Union through the ARI program.

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