1plg
From Proteopedia
(New page: 200px<br /><applet load="1plg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1plg, resolution 2.8Å" /> '''EVIDENCE FOR THE EXTE...) |
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| - | [[Image:1plg.gif|left|200px]]<br /><applet load="1plg" size=" | + | [[Image:1plg.gif|left|200px]]<br /><applet load="1plg" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1plg, resolution 2.8Å" /> | caption="1plg, resolution 2.8Å" /> | ||
'''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'''<br /> | '''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'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The antigen binding fragment from an IgG2a kappa murine monoclonal | + | The antigen binding fragment from an IgG2a kappa murine monoclonal antibody with specificity for alpha-(2-->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. |
==About this Structure== | ==About this Structure== | ||
| - | 1PLG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1PLG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PLG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Altman, E.]] | [[Category: Altman, E.]] | ||
[[Category: Bitter-Suermann, D.]] | [[Category: Bitter-Suermann, D.]] | ||
| - | [[Category: Brisson, J | + | [[Category: Brisson, J R.]] |
| - | [[Category: Bundle, D | + | [[Category: Bundle, D R.]] |
| - | [[Category: Evans, S | + | [[Category: Evans, S V.]] |
[[Category: Frosch, M.]] | [[Category: Frosch, M.]] | ||
| - | [[Category: Jennings, H | + | [[Category: Jennings, H J.]] |
[[Category: Klebert, S.]] | [[Category: Klebert, S.]] | ||
[[Category: Kratzin, H.]] | [[Category: Kratzin, H.]] | ||
| - | [[Category: Rose, D | + | [[Category: Rose, D R.]] |
| - | [[Category: Sigurskjold, B | + | [[Category: Sigurskjold, B W.]] |
[[Category: To, R.]] | [[Category: To, R.]] | ||
| - | [[Category: Tse, W | + | [[Category: Tse, W C.]] |
[[Category: Vaesen, M.]] | [[Category: Vaesen, M.]] | ||
[[Category: Weisgerber, C.]] | [[Category: Weisgerber, C.]] | ||
| - | [[Category: Young, N | + | [[Category: Young, N M.]] |
[[Category: immunoglobulin]] | [[Category: immunoglobulin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:30:03 2008'' |
Revision as of 12:30, 21 February 2008
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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
Overview
The antigen binding fragment from an IgG2a kappa murine monoclonal antibody with specificity for alpha-(2-->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.
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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