2DVG

Crystal structure of peanut lectin GAL-ALPHA-1,6-GLC complex

2DVG の概要

• エントリーDOI: 10.2210/pdb2dvg/pdb
• 関連するPDBエントリー: 1V6I 1V6J 1V6K 2DH1 2DV9 2DVA 2DVB 2DVD 2DVF 2PEL 2TEP
• 分子名称: Galactose-binding lectin, alpha-D-galactopyranose-(1-6)-beta-D-glucopyranose, alpha-D-galactopyranose, ... (7 entities in total)
• 機能のキーワード: legume lectin, agglutinin, open quaternary structure, carbohydrate specificity, sugar binding protein
• 由来する生物種: Arachis hypogaea (peanut)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 102290.78

構造登録者

Natchiar, S.K.,Srinivas, O.,Mitra, N.,Surolia, A.,Jayaraman, N.,Vijayan, M. (登録日: 2006-07-31, 公開日: 2006-11-07, 最終更新日: 2023-10-25)

主引用文献

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

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: 17057347
DOI: 10.1107/S0907444906035712

実験手法

X-RAY DIFFRACTION (2.78 Å)