PDBsum entry 1url

Sugar binding protein/immune system

PDB id: 1url

Contents

Protein chain

118 a.a. *

Ligands

GLY-HIS-THR-TRP-GLY-HIA

SIA

Waters ×18

* Residue conservation analysis

PDB id:

1url

Name:

Sugar binding protein/immune system

Title:

N-terminal domain of sialoadhesin (mouse) in complex with glycopeptide

Structure:

Sialoadhesin. Chain: a. Fragment: n-terminal domain, residues 20-137. Synonym: sialic acid binding ig-like lectin-1, siglec-1. Engineered: yes. Ala-gly-his-thr-trp-gly-hia. Chain: b. Engineered: yes. Other_details: hia is a modified histidine, o-sialic acid bound on

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Expressed in: cricetulus griseus. Expression_system_taxid: 10029. Synthetic: yes. Synthetic construct. Organism_taxid: 32630

Biol. unit:

Dimer (from PDB file)

Resolution:

2.40Å R-factor: 0.225 R-free: 0.273

Authors:

J.T.Bukrinsky,P.M.S.Hilaire,M.Meldal,P.R.Crocker,A.Henriksen

Key ref:

J.T.Bukrinsky et al. (2004). Complex of sialoadhesin with a glycopeptide ligand. Biochim Biophys Acta, 1702, 173-179. PubMed id: 15488769 DOI: 10.1016/j.bbapap.2004.08.015

Date:

31-Oct-03 Release date: 20-Oct-04

Protein chain

Q62230  (SN_MOUSE) -  Sialoadhesin from Mus musculus

Seq: 1695 a.a.

Struc: 118 a.a.

DOI no: 10.1016/j.bbapap.2004.08.015

Biochim Biophys Acta 1702:173-179 (2004)

PubMed id: 15488769

Complex of sialoadhesin with a glycopeptide ligand.

J.T.Bukrinsky, P.M.St Hilaire, M.Meldal, P.R.Crocker, A.Henriksen.

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.