1plg

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{{STRUCTURE_1plg| PDB=1plg | SCENE= }}
{{STRUCTURE_1plg| PDB=1plg | SCENE= }}
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'''EVIDENCE FOR THE EXTENDED HELICAL NATURE OF POLYSACCHARIDE EPITOPES. THE 2.8 ANGSTROMS RESOLUTION STRUCTURE AND THERMODYNAMICS OF LIGAND BINDING OF AN ANTIGEN BINDING FRAGMENT SPECIFIC FOR ALPHA-(2->8)-POLYSIALIC ACID'''
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===EVIDENCE FOR THE EXTENDED HELICAL NATURE OF POLYSACCHARIDE EPITOPES. THE 2.8 ANGSTROMS RESOLUTION STRUCTURE AND THERMODYNAMICS OF LIGAND BINDING OF AN ANTIGEN BINDING FRAGMENT SPECIFIC FOR ALPHA-(2->8)-POLYSIALIC ACID===
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==Overview==
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The antigen binding fragment from an IgG2a kappa murine monoclonal antibody with specificity for alpha-(2--&gt;8)-linked sialic acid polymers has been prepared and crystallized in the absence of hapten. Crystals were grown by vapor diffusion equilibrium with 16-18% polyethylene glycol 4000 solutions. The structure was solved by molecular replacement methods and refined to a conventional R factor of 0.164 for data to 2.8 A. The binding site is observed to display a shape and distribution of charges that is complementary to that of the predicted conformation of the oligosaccharide epitope. A thermodynamic description of ligand binding has been compiled for oligosaccharides ranging in length from 9 to 41 residues, and the data for the largest ligand has been used in a novel way to estimate the size of the antigen binding site. A model of antigen binding is presented that satisfies this thermodynamic data, as well as a previously reported requirement of conformational specificity of the oligosaccharide. X-ray crystallographic and thermodynamic evidence are consistent with a binding site that accommodates at least eight sialic acid residues.
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{{ABSTRACT_PUBMED_7538787}}
==About this Structure==
==About this Structure==
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[[Category: Young, N M.]]
[[Category: Young, N M.]]
[[Category: Immunoglobulin]]
[[Category: Immunoglobulin]]
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Revision as of 00:44, 29 July 2008

Image:1plg.png

Template:STRUCTURE 1plg

EVIDENCE FOR THE EXTENDED HELICAL NATURE OF POLYSACCHARIDE EPITOPES. THE 2.8 ANGSTROMS RESOLUTION STRUCTURE AND THERMODYNAMICS OF LIGAND BINDING OF AN ANTIGEN BINDING FRAGMENT SPECIFIC FOR ALPHA-(2->8)-POLYSIALIC ACID

Template:ABSTRACT PUBMED 7538787

About this Structure

1PLG is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

Evidence for the extended helical nature of polysaccharide epitopes. The 2.8 A resolution structure and thermodynamics of ligand binding of an antigen binding fragment specific for alpha-(2-->8)-polysialic acid., Evans SV, Sigurskjold BW, Jennings HJ, Brisson JR, To R, Tse WC, Altman E, Frosch M, Weisgerber C, Kratzin HD, et al., Biochemistry. 1995 May 23;34(20):6737-44. PMID:7538787

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