2dsu: Difference between revisions

Revision as of 00:54, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2dsu.png

Template:STRUCTURE 2dsu

Binding of chitin-like polysaccharide to protective signalling factor: Crystal structure of the complex formed between signalling protein from sheep (SPS-40) with a tetrasaccharide at 2.2 A resolutionBinding of chitin-like polysaccharide to protective signalling factor: Crystal structure of the complex formed between signalling protein from sheep (SPS-40) with a tetrasaccharide at 2.2 A resolution

Template:ABSTRACT PUBMED 17188513

About this StructureAbout this Structure

2DSU is a Single protein structure of sequence from Ovis aries. This structure supersedes the now removed PDB entry 2ao8. Full crystallographic information is available from OCA.

ReferenceReference

Carbohydrate binding properties and carbohydrate induced conformational switch in sheep secretory glycoprotein (SPS-40): crystal structures of four complexes of SPS-40 with chitin-like oligosaccharides., Srivastava DB, Ethayathulla AS, Kumar J, Somvanshi RK, Sharma S, Dey S, Singh TP, J Struct Biol. 2007 Jun;158(3):255-66. Epub 2006 Nov 17. PMID:17188513

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OCA

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-'''Binding of chitin-like polysaccharide to protective signalling factor: Crystal structure of the complex formed between signalling protein from sheep (SPS-40) with a tetrasaccharide at 2.2 A resolution'''
+===Binding of chitin-like polysaccharide to protective signalling factor: Crystal structure of the complex formed between signalling protein from sheep (SPS-40) with a tetrasaccharide at 2.2 A resolution===
-==Overview==
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-Crystal structures of four complexes of sheep secretory glycoprotein (SPS-40) with N-acetylglucosamine oligosaccharides (GlcNAc(n), (n=3-6)) have been determined at moderate resolutions. The binding studies of SPS-40 have been carried out using fluorescence spectroscopy and Surface Plasmon Resonance (SPR). Structure determinations of four complexes have shown a novel binding pattern of GlcNAc(n) molecules to SPS-40. The results indicate that the most preferred recognition region in the carbohydrate binding groove in SPS-40 is at subsites -4 to -2 among which subsite -2 provides the maximum interactions with carbohydrate residues. These structures have also shown that the interactions of GlcNAc3 and GlcNAc4 do not perturb the protein structure and those of GlcNAc5 induce partial conformational changes while in the case of GlcNAc6 the partially closed binding groove opened up completely. As in other SPX-40 structures, SPS-40 structure contains three overlapping flexible surface segments, His188-His197, Phe202-Arg212 and Phe244-Pro260 with several charged residues protruding outwardly. It creates a cluster of positive charges with a flexible base thus indicating a good scope of promoting the intermolecular interactions. This protein is glycosylated at Asn39 and may recognize other receptors having sugar binding sites. It appears that SPS-40 may involve both carbohydrate and protein bindings. The systematic carbohydrate-binding studies and the detailed structural results of four protein-carbohydrate complexes provide an excellent insight into the mechanism of carbohydrate binding. These are the first studies of this kind on secretory glycoproteins and their interactions with carbohydrates.
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 ==About this Structure==
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 [[Category: Oligosaccharide]]
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