1FAY

WINGED BEAN ACIDIC LECTIN COMPLEXED WITH METHYL-ALPHA-D-GALACTOSE (MONOCLINIC FORM)

1FAY の概要

• エントリーDOI: 10.2210/pdb1fay/pdb
• 関連するPDBエントリー: 1F9K
• 分子名称: ACIDIC LECTIN, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, methyl alpha-D-galactopyranoside, ... (6 entities in total)
• 機能のキーワード: legume lectin, glycosylated protein, h-antigenic specificity, agglutinin, sugar binding protein
• 由来する生物種: Psophocarpus tetragonolobus (winged bean)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 215980.97

構造登録者

Manoj, N.,Srinivas, V.R.,Surolia, A.,Vijayan, M.,Suguna, K. (登録日: 2000-07-14, 公開日: 2001-07-14, 最終更新日: 2024-10-30)

主引用文献

Manoj, N.,Srinivas, V.R.,Surolia, A.,Vijayan, M.,Suguna, K.
Carbohydrate specificity and salt-bridge mediated conformational change in acidic winged bean agglutinin.
J.Mol.Biol., 302:1129-1137, 2000

PubMed Abstract: Structures of two crystal forms of the dimeric acidic winged bean agglutinin (WBAII) complexed with methyl-alpha-D-galactose have been determined at 3.0 A and 3.3 A resolution. The subunit structure and dimerisation of the lectin are similar to those of the basic lectin from winged bean (WBAI) and the lectin from Erythrina corallodendron (EcorL). The conformation of a loop and its orientation with respect to the rest of the molecule in WBAII are, however, different from those in all the other legume lectins of known structure. This difference appears to have been caused by the formation of two strategically placed salt bridges in the former. Modelling based on the crystal structures provides a rationale for the specificity of the lectin, which is very different from that of WBAI, for the H-antigenic determinant responsible for O blood group reactivity. It also leads to a qualitative explanation for the thermodynamic data on sugar-binding to the lectin, with special emphasis on the role of a tyrosyl residue in the variable loop in the sugar-binding region in generating the carbohydrate specificity of WBAII.

PubMed: 11183779
DOI: 10.1006/jmbi.2000.4111

実験手法

X-RAY DIFFRACTION (3.3 Å)