1plg: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1plg]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PLG FirstGlance]. <br>
<table><tr><td colspan='2'>[[1plg]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PLG FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1plg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1plg OCA], [https://pdbe.org/1plg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1plg RCSB], [https://www.ebi.ac.uk/pdbsum/1plg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1plg ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1plg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1plg OCA], [https://pdbe.org/1plg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1plg RCSB], [https://www.ebi.ac.uk/pdbsum/1plg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1plg ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GCAM_MOUSE GCAM_MOUSE]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1plg ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1plg ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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--&gt;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<ref>PMID:7538787</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1plg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Altman, E]]
[[Category: Altman E]]
[[Category: Bitter-Suermann, D]]
[[Category: Bitter-Suermann D]]
[[Category: Brisson, J R]]
[[Category: Brisson J-R]]
[[Category: Bundle, D R]]
[[Category: Bundle DR]]
[[Category: Evans, S V]]
[[Category: Evans SV]]
[[Category: Frosch, M]]
[[Category: Frosch M]]
[[Category: Jennings, H J]]
[[Category: Jennings HJ]]
[[Category: Klebert, S]]
[[Category: Klebert S]]
[[Category: Kratzin, H]]
[[Category: Kratzin H]]
[[Category: Rose, D R]]
[[Category: Rose DR]]
[[Category: Sigurskjold, B W]]
[[Category: Sigurskjold BW]]
[[Category: To, R]]
[[Category: To R]]
[[Category: Tse, W C]]
[[Category: Tse WC]]
[[Category: Vaesen, M]]
[[Category: Vaesen M]]
[[Category: Weisgerber, C]]
[[Category: Weisgerber C]]
[[Category: Young, N M]]
[[Category: Young NM]]
[[Category: Immunoglobulin]]

Revision as of 05:56, 17 April 2024

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

1plg, resolution 2.80Å

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