1qdo: Difference between revisions

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[[Image:1qdo.jpg|left|200px]]
{{Seed}}
[[Image:1qdo.png|left|200px]]


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{{STRUCTURE_1qdo|  PDB=1qdo  |  SCENE=  }}  
{{STRUCTURE_1qdo|  PDB=1qdo  |  SCENE=  }}  


'''MAN(APLHA1-3)MAN(ALPHA1-O)METHYL CONCANAVALIN A COMPLEX'''
===MAN(APLHA1-3)MAN(ALPHA1-O)METHYL CONCANAVALIN A COMPLEX===




==Overview==
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The crystal structures of concanavalin A in complex with Man(alpha1-6)Man(alpha1-O)Me and Man(alpha1-3)Man(alpha1-O)Me were determined at resolutions of 2.0 and 2.8 A, respectively. In both structures, the O-1-linked mannose binds in the conserved monosaccharide-binding site. The O-3-linked mannose of Man(alpha1-3)Man(alpha1-O)Me binds in the hydrophobic subsite formed by Tyr-12, Tyr-100, and Leu-99. The shielding of a hydrophobic surface is consistent with the associated large heat capacity change. The O-6-linked mannose of Man(alpha1-6)Man(alpha1-O)Me binds in the same subsite formed by Tyr-12 and Asp-16 as the reducing mannose of the highly specific trimannose Man(alpha1-3)[Man(alpha1-6)]Man(alpha1-O)Me. However, it is much less tightly bound. Its O-2 hydroxyl makes no hydrogen bond with the conserved water 1. Water 1 is present in all the sugar-containing concanavalin A structures and increases the complementarity between the protein-binding surface and the sugar, but is not necessarily a hydrogen-bonding partner. A water analysis of the carbohydrate-binding site revealed a conserved water molecule replacing O-4 on the alpha1-3-linked arm of the trimannose. No such water is found for the reducing or O-6-linked mannose. Our data indicate that the central mannose of Man(alpha1-3)[Man(alpha1-6)]Man(alpha1-O)Me primarily functions as a hinge between the two outer subsites.
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{{ABSTRACT_PUBMED_10506175}}


==About this Structure==
==About this Structure==
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[[Category: Dimannose]]
[[Category: Dimannose]]
[[Category: Plant lectin]]
[[Category: Plant lectin]]
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