1MVQ

Cratylia mollis lectin (isoform 1) in complex with methyl-alpha-D-mannose

1MVQ の概要

• エントリーDOI: 10.2210/pdb1mvq/pdb
• 分子名称: lectin, isoform 1, methyl alpha-D-mannopyranoside, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: legume lectin, sugar binding protein
• 由来する生物種: Cratylia mollis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25683.20

構造登録者

de Souza, G.A.,Oliveira, P.S.,Trapani, S.,Correia, M.T.,Oliva, G.,Coelho, L.C.,Greene, L.J. (登録日: 2002-09-26, 公開日: 2003-10-07, 最終更新日: 2024-02-14)

主引用文献

De Souza, G.A.,Oliveira, P.S.,Trapani, S.,Santos, A.C.,Rosa, J.C.,Laure, H.J.,Correia, M.T.,Tavares, G.A.,Oliva, G.,Coelho, L.C.,Greene, L.J.
Amino acid sequence and tertiary structure of Cratylia mollis seed lectin
Glycobiology, 13:961-972, 2003

PubMed Abstract: Carbohydrate-protein interactions play a key role in many biological processes. Cramoll is a lectin purified from Cratylia mollis seeds that is taxonomically related to concanavalin A (Con A). Although Cramoll and Con A have the same monosaccharide specificity, they have different glycoprotein binding profiles. We report the primary structure of Cramoll, determined by Edman degradation and mass spectrometry and its 1.77 A crystallographic structure and compare it with the three-dimensional structure of Con A in an attempt to understand how differential binding can be achieved by similar or nearly identical structures. We report here that Cramoll consists of 236 residues, with 82% identity with Con A, and that its topological architecture is essentially identical to Con A, because the Calpha positional differences are below 3.5 A. Cramoll and Con A have identical binding sites for MealphaMan, Mn2+, and Ca2+. However, we observed six substitutions in a groove adjacent to the extended binding site and two in the extended binding site that may explain the differences in binding of oligosaccharides and glycoproteins between Cramoll and Con A.

PubMed: 12966038
DOI: 10.1093/glycob/cwg115

実験手法

X-RAY DIFFRACTION (1.77 Å)