3wog: Difference between revisions
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==Crystal structure plant lectin in complex with ligand== | |||
=== | <StructureSection load='3wog' size='340' side='right' caption='[[3wog]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3wog]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Phaseolus_vulgaris Phaseolus vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WOG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WOG FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wcr|3wcr]], [[3wcs|3wcs]]</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=3wog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wog OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wog RCSB], [http://www.ebi.ac.uk/pdbsum/3wog PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Phytohemagglutinin from Phaseolus vulgaris (PHA-E), a legume lectin, has an unusual specificity toward biantennary galactosylated N-glycan with bisecting N-acetylglucosamine (GlcNAc). To investigate the interaction in detail, we have solved the crystal structures of PHA-E without ligand and in complex with biantennary N-glycan derivatives. PHA-E interacts with the trisaccharide unit (Galbeta1-4GlcNAcbeta1-2Man) in a manner completely different from that of mannose/glucose-specific legume lectins. The inner mannose residue binds to a novel site on the protein, and its rotation is opposite to that occurring in the monosaccharide-binding site of other lectins around the sugar O3 axis. Saturation-transfer difference NMR using biantennary di-galactosylated and bisected glycans reveals that PHA-E interacts with both antennas almost equally. The unique carbohydrate interaction explains the glycan-binding specificity and high affinity. | |||
Phytohemagglutinin from Phaseolus vulgaris (PHA-E) displays a novel glycan recognition mode using a common legume lectin fold.,Nagae M, Soga K, Morita-Matsumoto K, Hanashima S, Ikeda A, Yamamoto K, Yamaguchi Y Glycobiology. 2014 Apr;24(4):368-78. doi: 10.1093/glycob/cwu004. Epub 2014 Jan, 16. PMID:24436051<ref>PMID:24436051</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Phaseolus vulgaris]] | [[Category: Phaseolus vulgaris]] | ||
[[Category: Nagae, M | [[Category: Nagae, M]] | ||
[[Category: Yamaguchi, Y | [[Category: Yamaguchi, Y]] | ||
[[Category: Complex-type n-glycan containing bisecting glcnac]] | [[Category: Complex-type n-glycan containing bisecting glcnac]] | ||
[[Category: Legume lectin]] | [[Category: Legume lectin]] | ||
[[Category: Sugar binding protein]] | [[Category: Sugar binding protein]] | ||
Revision as of 10:09, 4 January 2015
Crystal structure plant lectin in complex with ligand
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