2JWP

Malectin

2JWP の概要

• エントリーDOI: 10.2210/pdb2jwp/pdb
• 分子名称: Malectin (1 entity in total)
• 機能のキーワード: lectin, sugar binding, sugar binding protein
• 由来する生物種: Xenopus laevis (African clawed frog)
• 細胞内の位置: Endoplasmic reticulum membrane; Single-pass type I membrane protein: Q6INX3
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19538.08

構造登録者

Schallus, T.,Muhle-goll, C. (登録日: 2007-10-23, 公開日: 2008-08-12, 最終更新日: 2024-05-29)

主引用文献

Schallus, T.,Jaeckh, C.,Feher, K.,Palma, A.S.,Liu, Y.,Simpson, J.C.,Mackeen, M.,Stier, G.,Gibson, T.J.,Feizi, T.,Pieler, T.,Muhle-Goll, C.
Malectin: A Novel Carbohydrate-binding Protein of the Endoplasmic Reticulum and a Candidate Player in the Early Steps of Protein N-Glycosylation
Mol.Cell.Biol., 19:3404-3414, 2008

PubMed Abstract: N-Glycosylation starts in the endoplasmic reticulum (ER) where a 14-sugar glycan composed of three glucoses, nine mannoses, and two N-acetylglucosamines (Glc(3)Man(9)GlcNAc(2)) is transferred to nascent proteins. The glucoses are sequentially trimmed by ER-resident glucosidases. The Glc(3)Man(9)GlcNAc(2) moiety is the substrate for oligosaccharyltransferase; the Glc(1)Man(9)GlcNAc(2) and Man(9)GlcNAc(2) intermediates are signals for glycoprotein folding and quality control in the calnexin/calreticulin cycle. Here, we report a novel membrane-anchored ER protein that is highly conserved in animals and that recognizes the Glc(2)-N-glycan. Structure determination by nuclear magnetic resonance showed that its luminal part is a carbohydrate binding domain that recognizes glucose oligomers. Carbohydrate microarray analyses revealed a uniquely selective binding to a Glc(2)-N-glycan probe. The localization, structure, and binding specificity of this protein, which we have named malectin, open the way to studies of its role in the genesis, processing and secretion of N-glycosylated proteins.

PubMed: 18524852
DOI: 10.1091/mbc.E08-04-0354

実験手法

SOLUTION NMR