2e51

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[[Image:2e51.gif|left|200px]]<br /><applet load="2e51" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2e51.gif|left|200px]]
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caption="2e51, resolution 2.50&Aring;" />
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'''Crystal structure of basic winged bean lectin in complex with A blood group disaccharide'''<br />
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{{Structure
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|PDB= 2e51 |SIZE=350|CAPTION= <scene name='initialview01'>2e51</scene>, resolution 2.50&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''Crystal structure of basic winged bean lectin in complex with A blood group disaccharide'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2E51 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Psophocarpus_tetragonolobus Psophocarpus tetragonolobus] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E51 OCA].
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2E51 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Psophocarpus_tetragonolobus Psophocarpus tetragonolobus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E51 OCA].
==Reference==
==Reference==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=17510954 17510954]
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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]
[[Category: Psophocarpus tetragonolobus]]
[[Category: Psophocarpus tetragonolobus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: sugar binding protein]]
[[Category: sugar binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:06:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:35:23 2008''

Revision as of 14:35, 20 March 2008


PDB ID 2e51

Drag the structure with the mouse to rotate
, resolution 2.50Å
Ligands: and
Coordinates: save as pdb, mmCIF, xml



Crystal structure of basic winged bean lectin in complex with A 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.

About this Structure

2E51 is a Single protein structure of sequence from Psophocarpus tetragonolobus. Full crystallographic information is available from OCA.

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:17510954

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