2KR2

Xenopus laevis malectin complexed with maltose (Glcalpha1-4Glc)

2KR2 の概要

• エントリーDOI: 10.2210/pdb2kr2/pdb
• 関連するPDBエントリー: 2JWP 2K46
• 関連するBIRD辞書のPRD_ID: PRD_900018
• 分子名称: Malectin-A, alpha-D-glucopyranose-(1-4)-beta-D-glucopyranose (2 entities in total)
• 機能のキーワード: lectin/carbohydrate, carbohydrate metabolism, endoplasmic reticulum, glycoprotein, membrane, transmembrane, carbohydrate binding protein
• 由来する生物種: Xenopus laevis (clawed frog,common platanna,platanna)
• 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: 21542.30

構造登録者

Schallus, T.,Feher, K.,Muhle-Goll, C. (登録日: 2009-11-30, 公開日: 2010-07-14, 最終更新日: 2024-05-01)

主引用文献

Schallus, T.,Feher, K.,Sternberg, U.,Rybin, V.,Muhle-Goll, C.
Analysis of the specific interactions between the lectin domain of malectin and diglucosides.
Glycobiology, 20:1010-1020, 2010

PubMed Abstract: The endoplasmic reticulum malectin is a highly conserved protein in the animal kingdom that has no counterpart so far in lower organisms. We recently determined the structure of its conserved domain and found a highly selective binding to Glc(2)Man(9)GlcNAc(2), an intermediate of N-glycosylation. In our quest for putative ligands during the initial characterization of the protein, we noticed that the malectin domain is highly specific for diglucosides but quite tolerant towards the linkage of the glucosidic bond. To understand the molecular requirements for the observed promiscuity of the malectin domain, here we analyze the binding to a range of diglucosides through comparison of the protein chemical shift perturbation patterns and the saturation transfer difference spectra of the ligands including two maltose-mimicking drugs. A comparison of the maltose-bound structure of the malectin domain with the complex of the native ligand nigerose reveals why malectin is able to tolerate such a diversity of ligands.

PubMed: 20466650
DOI: 10.1093/glycob/cwq059

実験手法

SOLUTION NMR