1cvn
From Proteopedia
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| - | [[Image:1cvn.gif|left|200px]] | + | [[Image:1cvn.gif|left|200px]] |
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| - | '''CONCANAVALIN A COMPLEXED TO TRIMANNOSIDE''' | + | {{Structure |
| + | |PDB= 1cvn |SIZE=350|CAPTION= <scene name='initialview01'>1cvn</scene>, resolution 2.3Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CONCANAVALIN A COMPLEXED TO TRIMANNOSIDE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CVN is a [ | + | 1CVN 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=1CVN OCA]. |
==Reference== | ==Reference== | ||
| - | Structural basis of trimannoside recognition by concanavalin A., Naismith JH, Field RA, J Biol Chem. 1996 Jan 12;271(2):972-6. PMID:[http:// | + | Structural basis of trimannoside recognition by concanavalin A., Naismith JH, Field RA, J Biol Chem. 1996 Jan 12;271(2):972-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8557713 8557713] |
[[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: lectin (agglutinin)]] | [[Category: lectin (agglutinin)]] | ||
[[Category: saccharide binding]] | [[Category: saccharide binding]] | ||
| - | ''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 10:29:28 2008'' |
Revision as of 08:29, 20 March 2008
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| , resolution 2.3Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CONCANAVALIN A COMPLEXED TO TRIMANNOSIDE
Overview
Despite the fact that complex saccharides play an important role in many biological recognition processes, molecular level descriptions of protein-carbohydrate interactions are sparse. The legume lectin concanavalin A (con A), from Canavalia ensiformis, specifically recognizes the trimannoside core of many complex glycans. We have determined the crystal structure of a con A-trimannoside complex at 2.3-A resolution now describe the trimannoside interaction with conA. All three sugar residues are in well defined difference electron density. The 1,6-linked mannose residue is bound at the previously reported monosaccharide binding site; the other two sugars bind in an extended cleft formed by residues Tyr-12, Pro-13, Asn-14, Thr-15, and Asp-16. Hydrogen bonds are formed between the protein and all three sugar residues. In particular, the 1,3-linked mannose residue makes a strong hydrogen bond with the main chain of the protein. In addition, a water molecule, which is conserved in other con A structures, plays an important role in anchoring the reducing sugar unit to the protein. The complex is further stabilized by van der Waals interactions. The structure provides a rationale for the high affinity of con A for N-linked glycans.
About this Structure
1CVN is a Single protein structure of sequence from Canavalia ensiformis. Full crystallographic information is available from OCA.
Reference
Structural basis of trimannoside recognition by concanavalin A., Naismith JH, Field RA, J Biol Chem. 1996 Jan 12;271(2):972-6. PMID:8557713
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