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2cwg

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Revision as of 02:38, 10 September 2015

CRYSTALLOGRAPHIC REFINEMENT AND STRUCTURE ANALYSIS OF THE COMPLEX OF WHEAT GERM AGGLUTININ WITH A BIVALENT SIALOGLYCOPEPTIDE FROM GLYCOPHORIN A

Structural highlights

2cwg is a 4 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:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[AGI1_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

Wheat germ agglutinin (WGA) elicits a number of biological effects in erythrocytes as a result of specific binding to the transmembrane protein glycophorin A. The structure of co-crystals of WGA (isolectin 1: WGA1) with a bivalent sialoglycopeptide fragment of glycophorin A (T5), determined at 2.0 A resolution, has been further refined and analyzed with respect to ligand-induced changes in the tertiary structure, mobility, solvation, saccharide conformation and protein/saccharide interactions at three independent N-acetyl-D-neuraminic (NeuNAc) binding sites. The final model, which includes the two independent WGA1 monomers (composed of domains A, B, C and D), two positions for bound T5 sialo-tetrasaccharide (NeuNAc-alpha 2,3-Gal-beta 1,3-(alpha 2,6-NeuNAc)GalNAc) and 386 water molecules, refined to a crystallographic R-factor of 17.1% (Fo > 1.0 sigma) and an average temperature factor of 31.99 A2. Comparisons between the tertiary structures of the liganded and unliganded WGA1 dimers indicate that the largest deviations from 2-fold symmetry are localized in domains engaged in sugar binding (B1 and C2) and at the C-terminal domain of monomer II (D2), forming a strong lattice contact. Interactions of the tetrasaccharide with amino acid ligands in the three binding sites and with water were carefully analyzed and compared. Bound conformations of terminal NeuNAc match to within a root-mean-square delta r of 0.3 A. The specificity-determining N-acetyl group superimposes best in comparison with other substituents of the sugar ring. Of the five domain binding sites that are not occupied in this dimeric crosslinked complex, only one is accessible to the NeuNAc monosaccharide as determined from a difference Fourier map at 3.0 A resolution.

Crystallographic refinement and structure analysis of the complex of wheat germ agglutinin with a bivalent sialoglycopeptide from glycophorin A.,Wright CS, Jaeger J J Mol Biol. 1993 Jul 20;232(2):620-38. PMID:8345526^[1]

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

References

↑ Wright CS, Jaeger J. Crystallographic refinement and structure analysis of the complex of wheat germ agglutinin with a bivalent sialoglycopeptide from glycophorin A. J Mol Biol. 1993 Jul 20;232(2):620-38. PMID:8345526 doi:http://dx.doi.org/10.1006/jmbi.1993.1415

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/2cwg"

Categories: Triticum aestivum | Wright, C S

@@ Line 5: / Line 5: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene></td></tr>
 <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>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></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=2cwg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cwg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cwg RCSB], [http://www.ebi.ac.uk/pdbsum/2cwg 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=2cwg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cwg OCA], [http://pdbe.org/2cwg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cwg RCSB], [http://www.ebi.ac.uk/pdbsum/2cwg PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 27: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2cwg" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

2cwg

From Proteopedia

Revision as of 02:38, 10 September 2015

CRYSTALLOGRAPHIC REFINEMENT AND STRUCTURE ANALYSIS OF THE COMPLEX OF WHEAT GERM AGGLUTININ WITH A BIVALENT SIALOGLYCOPEPTIDE FROM GLYCOPHORIN A

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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