1CVN
CONCANAVALIN A COMPLEXED TO TRIMANNOSIDE
Summary for 1CVN
| Entry DOI | 10.2210/pdb1cvn/pdb |
| Descriptor | CONCANAVALIN A, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose, MANGANESE (II) ION, ... (5 entities in total) |
| Functional Keywords | concanavalin a, saccharide binding, lectin (agglutinin) |
| Biological source | Canavalia ensiformis (jack bean) |
| Total number of polymer chains | 4 |
| Total formula weight | 104887.36 |
| Authors | Naismith, J.H. (deposition date: 1995-08-09, release date: 1996-10-14, Last modification date: 2024-05-22) |
| Primary citation | Naismith, J.H.,Field, R.A. Structural basis of trimannoside recognition by concanavalin A. J.Biol.Chem., 271:972-976, 1996 Cited by PubMed Abstract: 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. PubMed: 8557713DOI: 10.1074/jbc.271.2.972 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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