3wcr
From Proteopedia
(Difference between revisions)
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| - | + | ==Crystal structure of plant lectin (ligand-free form)== | |
| - | + | <StructureSection load='3wcr' size='340' side='right' caption='[[3wcr]], [[Resolution|resolution]] 2.45Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3wcr]] 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=3WCR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WCR FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wcs|3wcs]], [[3wog|3wog]]</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=3wcr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wcr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wcr RCSB], [http://www.ebi.ac.uk/pdbsum/3wcr 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> | |
| + | |||
| + | ==See Also== | ||
| + | *[[Hemagglutinin|Hemagglutinin]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Phaseolus vulgaris]] | [[Category: Phaseolus vulgaris]] | ||
| - | [[Category: Nagae, M | + | [[Category: Nagae, M]] |
| - | [[Category: Yamaguchi, Y | + | [[Category: Yamaguchi, Y]] |
[[Category: Carbohydrate binding]] | [[Category: Carbohydrate binding]] | ||
[[Category: Legume lectin fold]] | [[Category: Legume lectin fold]] | ||
[[Category: N-glycan]] | [[Category: N-glycan]] | ||
[[Category: Sugar binding protein]] | [[Category: Sugar binding protein]] | ||
Revision as of 07:28, 15 February 2015
Crystal structure of plant lectin (ligand-free form)
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