2DVD
Crystal structure of peanut lectin GAL-ALPHA-1,3-GAL complex
Summary for 2DVD
| Entry DOI | 10.2210/pdb2dvd/pdb |
| Related | 1V6I 1V6J 1V6K 2DH1 2DV9 2DVA 2DVB 2DVF 2DVG 2PEL 2TEP |
| Descriptor | Galactose-binding lectin, beta-D-galactopyranose-(1-3)-beta-D-galactopyranose, CALCIUM ION, ... (6 entities in total) |
| Functional Keywords | legume lectin, agglutinin, open quaternary structure, carbohydrate specificity, sugar binding protein |
| Biological source | Arachis hypogaea (peanut) |
| Total number of polymer chains | 4 |
| Total formula weight | 102969.32 |
| Authors | Natchiar, S.K.,Srinivas, O.,Mitra, N.,Surolia, A.,Jayaraman, N.,Vijayan, M. (deposition date: 2006-07-31, release date: 2006-11-07, Last modification date: 2023-10-25) |
| Primary citation | Natchiar, S.K.,Srinivas, O.,Mitra, N.,Surolia, A.,Jayaraman, N.,Vijayan, M. Structural studies on peanut lectin complexed with disaccharides involving different linkages: further insights into the structure and interactions of the lectin ACTA CRYSTALLOGR.,SECT.D, 62:1413-1421, 2006 Cited by PubMed Abstract: Crystal structures of peanut lectin complexed with Galbeta1-3Gal, methyl-T-antigen, Galbeta1-6GalNAc, Galalpha1-3Gal and Galalpha1-6Glc and that of a crystal grown in the presence of Galalpha1-3Galbeta1-4Gal have been determined using data collected at 100 K. The use of water bridges as a strategy for generating carbohydrate specificity was previously deduced from the complexes of the lectin with lactose (Galbeta1-4Glc) and T-antigen (Galbeta1-3GalNAc). This has been confirmed by the analysis of the complexes with Galbeta1-3Gal and methyl-T-antigen (Galbeta1-3GalNAc-alpha-OMe). A detailed analysis of lectin-sugar interactions in the complexes shows that they are more extensive when the beta-anomer is involved in the linkage. As expected, the second sugar residue is ill-defined when the linkage is 1-->6. There are more than two dozen water molecules which occur in the hydration shells of all structures determined at resolutions better than 2.5 A. Most of them are involved in stabilizing the structure, particularly loops. Water molecules involved in lectin-sugar interactions are also substantially conserved. The lectin molecule is fairly rigid and does not appear to be affected by changes in temperature. PubMed: 17057347DOI: 10.1107/S0907444906035712 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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