1GV9

p58/ERGIC-53

1GV9 の概要

• エントリーDOI: 10.2210/pdb1gv9/pdb
• 分子名称: P58/ERGIC-53, SULFATE ION (3 entities in total)
• 機能のキーワード: lectin, carbohydrate binding
• 由来する生物種: RATTUS NORVEGICUS (RAT)
• 細胞内の位置: Endoplasmic reticulum-Golgi intermediate compartment membrane ; Single-pass type I membrane protein : Q62902
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28493.45

構造登録者

Velloso, L.M.,Svensson, K.,Schneider, G.,Pettersson, R.F.,Lindqvist, Y. (登録日: 2002-02-07, 公開日: 2002-02-28, 最終更新日: 2024-10-23)

主引用文献

Velloso, L.M.,Svensson, K.,Schneider, G.,Pettersson, R.F.,Lindqvist, Y.
Crystal Structure of the Carbohydrate Recognition Domain of P58/Ergic-53, a Protein Involved in Glycoprotein Export from the Endoplasmic Reticulum.
J.Biol.Chem., 277:15979-, 2002

PubMed Abstract: p58/ERGIC-53 is an animal calcium-dependent lectin that cycles between the endoplasmic reticulum (ER) and the Golgi complex and appears to act as a cargo receptor for a subset of soluble glycoproteins exported from the ER. We have determined the crystal structure of the carbohydrate recognition domain (CRD) of p58, the rat homologue of human ERGIC-53, to 1.46 A resolution. The fold and ligand binding site are most similar to those of leguminous lectins. The structure also resembles that of the CRD of the ER folding chaperone calnexin and the neurexins, a family of non-lectin proteins expressed on neurons. The CRD comprises one concave and one convex beta-sheet packed into a beta-sandwich. The ligand binding site resides in a negatively charged cleft formed by conserved residues. A large surface patch of conserved residues with a putative role in protein-protein interactions and oligomerization lies on the opposite side of the ligand binding site. Together with previous functional data, the structure defines a new and expanding class of calcium-dependent animal lectins and provides a starting point for the understanding of glycoprotein sorting between the ER and the Golgi.

PubMed: 11850423
DOI: 10.1074/JBC.M112098200

実験手法

X-RAY DIFFRACTION (1.46 Å)