1i3h
From Proteopedia
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- | [[Image:1i3h.gif|left|200px]] | + | [[Image:1i3h.gif|left|200px]] |
- | + | ||
- | '''CONCANAVALIN A-DIMANNOSE STRUCTURE''' | + | {{Structure |
+ | |PDB= 1i3h |SIZE=350|CAPTION= <scene name='initialview01'>1i3h</scene>, resolution 1.2Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''CONCANAVALIN A-DIMANNOSE STRUCTURE''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1I3H is a [ | + | 1I3H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I3H OCA]. |
==Reference== | ==Reference== | ||
- | The 1.2 A resolution structure of the Con A-dimannose complex., Sanders DA, Moothoo DN, Raftery J, Howard AJ, Helliwell JR, Naismith JH, J Mol Biol. 2001 Jul 20;310(4):875-84. PMID:[http:// | + | The 1.2 A resolution structure of the Con A-dimannose complex., Sanders DA, Moothoo DN, Raftery J, Howard AJ, Helliwell JR, Naismith JH, J Mol Biol. 2001 Jul 20;310(4):875-84. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11453694 11453694] |
[[Category: Canavalia ensiformis]] | [[Category: Canavalia ensiformis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: CA]] | [[Category: CA]] | ||
[[Category: MN]] | [[Category: MN]] | ||
- | [[Category: concanavalin | + | [[Category: concanavalin some]] |
[[Category: protein-sugar complex]] | [[Category: protein-sugar complex]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:45:05 2008'' |
Revision as of 09:45, 20 March 2008
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, resolution 1.2Å | |||||||
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Ligands: | and | ||||||
Coordinates: | save as pdb, mmCIF, xml |
CONCANAVALIN A-DIMANNOSE STRUCTURE
Overview
The complex between concanavalin A (Con A) and alpha1-2 mannobiose (mannose alpha1-2 mannose) has been refined to 1.2 A resolution. This is the highest resolution structure reported for any sugar-lectin complex. As the native structure of Con A to 0.94 A resolution is already in the database, this gives us a unique opportunity to examine sugar-protein binding at high resolution. These data have allowed us to model a number of hydrogen atoms involved in the binding of the sugar to Con A, using the difference density map to place the hydrogen atoms. This map reveals the presence of the protonated form of Asp208 involved in binding. Asp208 is not protonated in the 0.94 A native structure. Our results clearly show that this residue is protonated and hydrogen bonds to the sugar. The structure accounts for the higher affinity of the alpha1-2 linked sugar when compared to other disaccharides. This structure identifies different interactions to those predicted by previous modelling studies. We believe that the additional data presented here will enable significant improvements to be made to the sugar-protein modelling algorithms.
About this Structure
1I3H is a Single protein structure of sequence from Canavalia ensiformis. Full crystallographic information is available from OCA.
Reference
The 1.2 A resolution structure of the Con A-dimannose complex., Sanders DA, Moothoo DN, Raftery J, Howard AJ, Helliwell JR, Naismith JH, J Mol Biol. 2001 Jul 20;310(4):875-84. PMID:11453694
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