2e53: Difference between revisions

Revision as of 13:22, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2e53.png

Template:STRUCTURE 2e53

Crystal structure of basic winged bean lectin in complex with B blood group disaccharideCrystal structure of basic winged bean lectin in complex with B blood group disaccharide

Template:ABSTRACT PUBMED 17510954

About this StructureAbout this Structure

2E53 is a Single protein structure of sequence from Psophocarpus tetragonolobus. Full crystallographic information is available from OCA.

ReferenceReference

Generation of blood group specificity: new insights from structural studies on the complexes of A- and B-reactive saccharides with basic winged bean agglutinin., Kulkarni KA, Katiyar S, Surolia A, Vijayan M, Suguna K, Proteins. 2007 Aug 15;68(3):762-9. PMID:17510954

Structural basis for the carbohydrate-specificity of basic winged-bean lectin and its differential affinity for Gal and GalNAc., Kulkarni KA, Katiyar S, Surolia A, Vijayan M, Suguna K, Acta Crystallogr D Biol Crystallogr. 2006 Nov;62(Pt 11):1319-24. Epub 2006, Oct 18. PMID:17057334

Carbohydrate specificity and quaternary association in basic winged bean lectin: X-ray analysis of the lectin at 2.5 A resolution., Prabu MM, Sankaranarayanan R, Puri KD, Sharma V, Surolia A, Vijayan M, Suguna K, J Mol Biol. 1998 Mar 6;276(4):787-96. PMID:9500920

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OCA

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 {{STRUCTURE_2e53|  PDB=2e53  |  SCENE=  }}
-'''Crystal structure of basic winged bean lectin in complex with B blood group disaccharide'''
+===Crystal structure of basic winged bean lectin in complex with B blood group disaccharide===
-==Overview==
+<!--
-Basic winged bean agglutinin binds A-blood group substance with higher affinity and B-blood group substance with lesser affinity. It does not bind the O substance. The crystal structures of the lectin, complexed with A-reactive and B-reactive di and tri saccharides, have been determined. In addition, the complexes of the lectin with fucosylated A-trisaccharides and B-trisaccharides and with a variant of the A-trisaccharide have been modeled. These structures and models provide valuable insights into the structural basis of blood group specificities. All the four carbohydrate binding loops of the lectin contribute to the primary combining site while the loop of variable length contributes to the secondary binding site. In a significant advance to the current understanding, the interactions at the secondary binding site also contribute substantially, albeit in a subtle manner, to determine the blood group specificity. Compared with the interactions of the B-trisaccharide with the lectin, the third sugar residue of the A-reactive trisacharide forms an additional hydrogen bond with a lysine residue in the variable loop. In the former, the formation of such a hydrogen bond is prevented by a shift in the orientation of third sugar resulting from an internal hydrogen bond in it. The formation of this bond is also facilitated by an interaction dependent change in the rotamer conformation of the lysyl residue of the variable loop. Thus, the difference in the interactions at the secondary site is generated by coordinated movements in the ligand as well as the protein. A comparison of the crystal structure and the model of the complex involving the variant of the A-trisaccharide results in the delineation of the relative contributions of the interactions at the primary and the secondary sites in determining blood group specificity.
+The line below this paragraph, {{ABSTRACT_PUBMED_17510954}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17510954 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17510954}}
 ==About this Structure==
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 ==Reference==
 Generation of blood group specificity: new insights from structural studies on the complexes of A- and B-reactive saccharides with basic winged bean agglutinin., Kulkarni KA, Katiyar S, Surolia A, Vijayan M, Suguna K, Proteins. 2007 Aug 15;68(3):762-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17510954 17510954]
+Structural basis for the carbohydrate-specificity of basic winged-bean lectin and its differential affinity for Gal and GalNAc., Kulkarni KA, Katiyar S, Surolia A, Vijayan M, Suguna K, Acta Crystallogr D Biol Crystallogr. 2006 Nov;62(Pt 11):1319-24. Epub 2006, Oct 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17057334 17057334]
+Carbohydrate specificity and quaternary association in basic winged bean lectin: X-ray analysis of the lectin at 2.5 A resolution., Prabu MM, Sankaranarayanan R, Puri KD, Sharma V, Surolia A, Vijayan M, Suguna K, J Mol Biol. 1998 Mar 6;276(4):787-96. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9500920 9500920]
 [[Category: Psophocarpus tetragonolobus]]
 [[Category: Single protein]]
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 [[Category: Jelly roll]]
 [[Category: Winged bean]]
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