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Naismith, James H. and Field, Robert A. 
ORCID: https://orcid.org/0000-0001-8574-0275
(1996)
Structural basis of trimannoside recognition by concanavalin A.
Journal of Biological Chemistry, 271 (2).
pp. 972-976.
ISSN 0021-9258
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-Å resolution and now describe the trimannoside interaction with con A. 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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | biochemistry,molecular biology,cell biology ,/dk/atira/pure/subjectarea/asjc/1300/1303 |
| Faculty \ School: | Faculty of Science > School of Chemistry, Pharmacy and Pharmacology |
| Related URLs: | |
| Depositing User: | LivePure Connector |
| Date Deposited: | 11 Sep 2024 14:30 |
| Last Modified: | 25 Sep 2024 18:09 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/96715 |
| DOI: | 10.1074/jbc.271.2.972 |
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