1cvn | pdb_00001cvn

CONCANAVALIN A COMPLEXED TO TRIMANNOSIDE

spinqualitylabelsall models 1cvn, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1cvn is a 4 chain structure with sequence from Canavalia ensiformis. The April 2010 RCSB PDB Molecule of the Month feature on Concanavalin A and Circular Permutation by David Goodsell is 10.2210/rcsb_pdb/mom_2010_4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: CA, MAN, MN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CONA_CANEN D-mannose specific lectin. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structural basis of trimannoside recognition by concanavalin A.,Naismith JH, Field RA J Biol Chem. 1996 Jan 12;271(2):972-6. PMID:8557713 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Concanavalin 3D structures

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