2hrl

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Revision as of 20:29, 12 November 2007

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spinqualitylabelsall models 2hrl, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Siglec-7 in complex with GT1b

Overview

The siglecs are a group of mammalian sialic acid binding receptors, expressed predominantly in the immune system. The CD33-related siglecs, show complex recognition patterns for sialylated glycans. Siglec-7 shows a, preference for alpha(2,8)-disialylated ligands and provides a structural, template for studying the key interactions that drive this selectivity. We, have co-crystallized Siglec-7 with a synthetic oligosaccharide, corresponding to the alpha(2,8)-disialylated ganglioside GT1b. The crystal, structure of the complex offers a first glimpse into how this important, family of lectins binds the structurally diverse gangliosides. The, structure reveals that the C-C' loop, a region implicated in previous, studies as driving siglec specificity, undergoes a dramatic conformational, shift, allowing it to interact with the underlying neutral glycan core of, the ganglioside. The structural data in combination with mutagenesis, studies show that binding of the ganglioside is driven by extensive, hydrophobic contacts together with key polar interactions and that the, binding site structure is complementary to preferred solution, conformations of GT1b.

About this Structure

2HRL is a Single protein structure of sequence from Homo sapiens with NAG and CEQ as ligands. Full crystallographic information is available from OCA.

Reference

Siglec-7 undergoes a major conformational change when complexed with the alpha(2,8)-disialylganglioside GT1b., Attrill H, Imamura A, Sharma RS, Kiso M, Crocker PR, van Aalten DM, J Biol Chem. 2006 Oct 27;281(43):32774-83. Epub 2006 Aug 8. PMID:16895906

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