4CSD

Structure of Monomeric Ralstonia solanacearum lectin

4CSD の概要

• エントリーDOI: 10.2210/pdb4csd/pdb
• 分子名称: FUCOSE-BINDING LECTIN PROTEIN, methyl alpha-L-fucopyranoside, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: fucose-binding protein, beta propeller
• 由来する生物種: RALSTONIA SOLANACEARUM
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 60930.12

構造登録者

Arnaud, J.,Trundle, K.,Claudinon, J.,Audfray, A.,Varrot, A.,Romer, W.,Imberty, A. (登録日: 2014-03-06, 公開日: 2014-10-08, 最終更新日: 2023-12-20)

主引用文献

Arnaud, J.,Trondle, K.,Claudinon, J.,Audfray, A.,Varrot, A.,Romer, W.,Imberty, A.
Membrane Deformation by Neolectins with Engineered Glycolipid Binding Sites.
Angew.Chem.Int.Ed.Engl., 53:9267-, 2014

PubMed Abstract: Lectins are glycan-binding proteins that are involved in the recognition of glycoconjugates at the cell surface. When binding to glycolipids, multivalent lectins can affect their distribution and alter membrane shapes. Neolectins have now been designed with controlled number and position of binding sites to decipher the role of multivalency on avidity to a glycosylated surface and on membrane dynamics of glycolipids. A monomeric hexavalent neolectin has been first engineered from a trimeric hexavalent bacterial lectin, From this neolectin template, 13 different neolectins with a valency ranging from 0 to 6 were designed, produced, and analyzed for their ability to bind fucose in solution, to attach to a glycosylated surface and to invaginate glycolipid-containing giant liposomes. Whereas the avidity only depends on the presence of at least two binding sites, the ability to bend and invaginate membranes critically depends on the distance between two adjacent binding sites.

PubMed: 25044646
DOI: 10.1002/ANIE.201404568

実験手法

X-RAY DIFFRACTION (1.35 Å)