1plg

<StructureSection load='1plg' size='340' side='right' caption='[[1plg]], [[Resolution|resolution]] 2.80&Aring;' scene=''>

<table><tr><td colspan='2'>[[1plg]] is a 2 chain structure with sequence 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1plg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1plg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1plg RCSB], [http://www.ebi.ac.uk/pdbsum/1plg PDBsum]</span></td></tr>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pl/1plg_consurf.spt"</scriptWhenChecked>

</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/chain_selection.php?pdb_ID=2ata ConSurf].

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== 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>

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== References ==

<references/>

[[Category: Altman, E]]

[[Category: Bitter-Suermann, D]]

[[Category: Brisson, J R]]

[[Category: Bundle, D R]]

[[Category: Evans, S V]]

[[Category: Frosch, M]]

[[Category: Jennings, H J]]

[[Category: Klebert, S]]

[[Category: Kratzin, H]]

[[Category: Rose, D R]]

[[Category: Sigurskjold, B W]]

[[Category: To, R]]

[[Category: Tse, W C]]

[[Category: Vaesen, M]]

[[Category: Weisgerber, C]]

[[Category: Young, N M]]

[[Category: Immunoglobulin]]