1qfp
From Proteopedia
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'''N-TERMINAL DOMAIN OF SIALOADHESIN (MOUSE)''' | '''N-TERMINAL DOMAIN OF SIALOADHESIN (MOUSE)''' | ||
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[[Category: May, A P.]] | [[Category: May, A P.]] | ||
[[Category: Robinson, R C.]] | [[Category: Robinson, R C.]] | ||
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Revision as of 03:12, 3 May 2008
N-TERMINAL DOMAIN OF SIALOADHESIN (MOUSE)
Overview
The structure of the functional N-terminal domain from the extracellular region of the cell surface receptor sialoadhesin has been determined in complex with the oligosaccharide 3' sialyllactose. This provides structural information for the siglec family of proteins. The structure conforms to the V-set immunoglobulin-like fold but contains several distinctive features, including an intra-beta sheet disulphide and a splitting of the standard beta strand G into two shorter strands. These novel features appear important in adapting the V-set fold for sialic acid-mediated recognition. Analysis of the complex with 3'sialyllactose highlights three residues, conserved throughout the siglec family, as key features of the sialic acid-binding template. The complex is representative of the functional recognition interaction with carbohydrate and as such provides detailed information for a heterotypic cell adhesion interaction.
About this Structure
1QFP is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Crystal structure of the N-terminal domain of sialoadhesin in complex with 3' sialyllactose at 1.85 A resolution., May AP, Robinson RC, Vinson M, Crocker PR, Jones EY, Mol Cell. 1998 Apr;1(5):719-28. PMID:9660955 Page seeded by OCA on Sat May 3 06:12:50 2008
