1cvn
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1cvn |SIZE=350|CAPTION= <scene name='initialview01'>1cvn</scene>, resolution 2.3Å | |PDB= 1cvn |SIZE=350|CAPTION= <scene name='initialview01'>1cvn</scene>, resolution 2.3Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cvn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cvn OCA], [http://www.ebi.ac.uk/pdbsum/1cvn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cvn RCSB]</span> | ||
}} | }} | ||
| Line 23: | Line 26: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Naismith, J H.]] | [[Category: Naismith, J H.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: MN]] | ||
[[Category: concanavalin some]] | [[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 | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:29:25 2008'' |
Revision as of 16:29, 30 March 2008
| |||||||
| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
Page seeded by OCA on Sun Mar 30 19:29:25 2008
