View source for 2lhx


==Di-O-GalNAc glycosylated Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat==
<StructureSection load='2lhx' size='340' side='right'caption='[[2lhx]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2lhx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LHX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LHX FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 24 models</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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=2lhx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lhx OCA], [https://pdbe.org/2lhx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lhx RCSB], [https://www.ebi.ac.uk/pdbsum/2lhx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lhx ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mucin glycoproteins present a complex structural landscape arising from the multiplicity of glycosylation patterns afforded by their numerous serine and threonine glycosylation sites, often in clusters, and with variations in respective glycans. To explore the structural complexities in such glycoconjugates, we used NMR to systematically analyze the conformational effects of glycosylation density within a cluster of sites. This allows correlation with molecular recognition through analysis of interactions between these and other glycopeptides, with antibodies, lectins, and sera, using a glycopeptide microarray. Selective antibody interactions with discrete conformational elements, reflecting aspects of the peptide and disposition of GalNAc residues, are observed. Our results help bridge the gap between conformational properties and molecular recognition of these molecules, with implications for their physiological roles. Features of the native mucin motifs impact their relative immunogenicity and are accurately encoded in the antibody binding site, with the conformational integrity being preserved in isolated glycopeptides, as reflected in the antibody binding profile to array components.

Deciphering structural elements of mucin glycoprotein recognition.,Borgert A, Heimburg-Molinaro J, Song X, Lasanajak Y, Ju T, Liu M, Thompson P, Ragupathi G, Barany G, Smith DF, Cummings RD, Live D ACS Chem Biol. 2012 Jun 15;7(6):1031-9. Epub 2012 Apr 9. PMID:22444368<ref>PMID:22444368</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2lhx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Barany G]]
[[Category: Borgert A]]
[[Category: Cummings R]]
[[Category: Heimburg-Molinaro J]]
[[Category: Ju T]]
[[Category: Lasanajak Y]]
[[Category: Liu M]]
[[Category: Live D]]
[[Category: Ragupathi G]]
[[Category: Smith D]]
[[Category: Thompson P]]