3PH9

Crystal structure of the human anterior gradient protein 3

3PH9 の概要

• エントリーDOI: 10.2210/pdb3ph9/pdb
• 分子名称: Anterior gradient protein 3 homolog (2 entities in total)
• 機能のキーワード: thioredoxin fold, protein disulfide isomerase, endoplasmic reticulum, isomerase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted (Probable): Q8TD06
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 35865.36

構造登録者

Nguyen, V.D.,Ruddock, L.W.,Salin, M.,Wierenga, R.K. (登録日: 2010-11-03, 公開日: 2011-10-19, 最終更新日: 2023-09-06)

主引用文献

Nguyen, V.D.,Biterova, E.,Salin, M.,Wierenga, R.K.,Ruddock, L.W.
Crystal structure of human anterior gradient protein 3.
Acta Crystallogr.,Sect.F, 74:425-430, 2018

PubMed Abstract: Oxidative protein folding in the endoplasmic reticulum is catalyzed by the protein disulfide isomerase family of proteins. Of the 20 recognized human family members, the structures of eight have been deposited in the PDB along with domains from six more. Three members of this family, ERp18, anterior gradient protein 2 (AGR2) and anterior gradient protein 3 (AGR3), are single-domain proteins which share sequence similarity. While ERp18 has a canonical active-site motif and is involved in native disulfide-bond formation, AGR2 and AGR3 lack elements of the active-site motif found in other family members and may both interact with mucins. In order to better define its function, the structure of AGR3 is required. Here, the recombinant expression, purification, crystallization and crystal structure of human AGR3 are described.

PubMed: 29969106
DOI: 10.1107/S2053230X18009093

実験手法

X-RAY DIFFRACTION (1.83 Å)