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1k7t

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Revision as of 15:31, 10 September 2015

Crystal Structure Analysis of crosslinked-WGA3/GlcNAcbeta1,6Gal complex

Structural highlights

1k7t is a 2 chain structure with sequence from Triticum aestivum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
Related:	1wgt, 1k7u, 1k7v
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[AGI3_WHEAT] N-acetyl-D-glucosamine / N-acetyl-D-neuraminic acid binding lectin.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The interactions of wheat-germ agglutinin (WGA) with the GlcNAc beta 1,6Gal sequence, a characteristic component of branched poly-N-acetyllactosaminoglycans, were investigated using isothermal titration calorimetry and X-ray crystallography. GlcNAc beta 1,6Gal exhibited an affinity greater than GlcNAc beta 1,4GlcNAc to all WGA isolectins, whereas Gal beta 1,6GlcNAc showed much less affinity than GlcNAc beta 1,4GlcNAc. X-ray structural analyses of the glutaraldehyde-crosslinked WGA isolectin 3 crystals in complex with GlcNAc beta 1,6Gal, GlcNAc beta 1,4GlcNAc and GlcNAc beta 1,6Gal beta 1,4Glc were performed at 2.4, 2.2 and 2.2 A resolution, respectively. In spite of different glycosidic linkages, GlcNAc beta 1,6Gal and GlcNAc beta 1,4GlcNAc exhibited basically similar binding modes to each other, in contact with side chains of two aromatic residues, Tyr64 and His66. However, the conformations of the ligands in the two primary binding sites were not always identical. GlcNAc beta 1,6Gal showed more extensive variation in the parameters defining the glycosidic linkage structure compared to GlcNAc beta 1,4GlcNAc, demonstrating large conformational flexibility of the former ligand in the interaction with WGA. The difference in the ligand binding conformation was accompanied by alterations of the side chain conformation of the amino acid residues involved in the interactions. The hydrogen bond between Ser62 and the non-reducing end GlcNAc was always observed regardless of the ligand type, indicating the key role of this interaction. In addition to the hydrogen bonding and van der Waals interactions, CH--pi interactions involving Tyr64, His66 and Tyr73 are suggested to play an essential role in determining the ligand binding conformation in all complexes. One of the GlcNAc beta 1,6Gal ligands had no crystal packing contact with another WGA molecule, therefore the conformation might be more relevant to the interaction mode in solution.

Interactions of wheat-germ agglutinin with GlcNAc beta 1,6Gal sequence.,Muraki M, Ishimura M, Harata K Biochim Biophys Acta. 2002 Jan 15;1569(1-3):10-20. PMID:11853952^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Muraki M, Ishimura M, Harata K. Interactions of wheat-germ agglutinin with GlcNAc beta 1,6Gal sequence. Biochim Biophys Acta. 2002 Jan 15;1569(1-3):10-20. PMID:11853952

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1k7t"

@@ Line 6: / Line 6: @@
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1wgt|1wgt]], [[1k7u|1k7u]], [[1k7v|1k7v]]</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=1k7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k7t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1k7t RCSB], [http://www.ebi.ac.uk/pdbsum/1k7t PDBsum]</span></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=1k7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k7t OCA], [http://pdbe.org/1k7t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1k7t RCSB], [http://www.ebi.ac.uk/pdbsum/1k7t PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 28: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1k7t" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

1k7t

From Proteopedia

Revision as of 15:31, 10 September 2015

Crystal Structure Analysis of crosslinked-WGA3/GlcNAcbeta1,6Gal complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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