1LEM

THE MONOSACCHARIDE BINDING SITE OF LENTIL LECTIN: AN X-RAY AND MOLECULAR MODELLING STUDY

1LEM の概要

• エントリーDOI: 10.2210/pdb1lem/pdb
• 分子名称: LECTIN, alpha-D-glucopyranose, CALCIUM ION, ... (6 entities in total)
• 機能のキーワード: lectin
• 由来する生物種: Lens culinaris (lentil); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 25896.44

構造登録者

Loris, R.,Wyns, L. (登録日: 1993-11-17, 公開日: 1994-01-31, 最終更新日: 2024-02-14)

主引用文献

Loris, R.,Casset, F.,Bouckaert, J.,Pletinckx, J.,Dao-Thi, M.H.,Poortmans, F.,Imberty, A.,Perez, S.,Wyns, L.
The monosaccharide binding site of lentil lectin: an X-ray and molecular modelling study.
Glycoconj.J., 11:507-517, 1994

PubMed Abstract: The X-ray crystal structure of lentil lectin in complex with alpha-D-glucopyranose has been determined by molecular replacement and refined to an R-value of 0.20 at 3.0 A resolution. The glucose interacts with the protein in a manner similar to that found in the mannose complexes of concanavalin A, pea lectin and isolectin I from Lathyrus ochrus. The complex is stabilized by a network of hydrogen bonds involving the carbohydrate oxygens O6, O4, O3 and O5. In addition, the alpha-D-glucopyranose residue makes van der Waals contacts with the protein, involving the phenyl ring of Phe123 beta. The overall structure of lentil lectin, at this resolution, does not differ significantly from the highly refined structures of the uncomplexed lectin. Molecular docking studies were performed with mannose and its 2-O and 3-O-m-nitro-benzyl derivatives to explain their high affinity binding. The interactions of the modelled mannose with lentil lectin agree well with those observed experimentally for the protein-carbohydrate complex. The highly flexible Me-2-O-(m-nitro-benzyl)-alpha-D-mannopyranoside and Me-3-O-(m-nitro-benzyl)-alpha-D-mannopyranoside become conformationally restricted upon binding to lentil lectin. For best orientations of the two substrates in the combining site, the loss of entropy is accompanied by the formation of a strong hydrogen bond between the nitro group and one amino acid, Gly97 beta and Asn125 beta, respectively, along with the establishment of van der Waals interactions between the benzyl group and the aromatic amino acids Tyr100 beta and Trp128 beta.

PubMed: 7696853
DOI: 10.1007/BF00731301

実験手法

X-RAY DIFFRACTION (3 Å)