Crystallographic and in silico analysis of the sialoside-binding characteristics of the Siglec sialoadhesin.

Journal article

The Siglec family of receptors mediates cell-surface interactions through recognition of sialylated glycoconjugates. Previously reported structures of the N-terminal domain of the Siglec sialoadhesin (SnD1) in complex with various sialic acid analogs revealed the structural template for sialic acid binding. To characterize further the carbohydrate-binding properties, we have determined the crystal structures of SnD1 in the absence of ligand, and in complex with 2-benzyl-Neu5NPro and 2-benzyl-...

Expand abstract

Authors: Zaccai, N; May, A; Robinson, R; Burtnick, L; Crocker, P

• Publication status: Published
• Journal: Journal of molecular biology
• Volume: 365
• Issue: 5
• Pages: 1469-1479
• Publication date: 2007-02-01
• DOI: 10.1016/j.jmb.2006.10.084
• EISSN: 1089-8638
• ISSN: 0022-2836
• Language: English
• Keywords: Membrane Glycoproteins; Protein Structure, Secondary; Models, Molecular; Animals; Receptors, Immunologic; Algorithms; Cricetinae; Cricetulus; Sialic Acid Binding Ig-like Lectin 1; Computational Biology; Crystallography, X-Ray; CHO Cells; Sialic Acids; Ligands