3RJO

Crystal Structure of ERAP1 Peptide Binding Domain

3RJO の概要

• エントリーDOI: 10.2210/pdb3rjo/pdb
• 分子名称: Endoplasmic reticulum aminopeptidase 1, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: erap1, aminopeptidase, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Endoplasmic reticulum membrane; Single-pass type II membrane protein (Probable): Q9NZ08
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 48839.88

構造登録者

Guo, H.-C.,Lakshminarasimhan, D.,Gandhi, A. (登録日: 2011-04-15, 公開日: 2011-12-21, 最終更新日: 2024-11-20)

主引用文献

Gandhi, A.,Lakshminarasimhan, D.,Sun, Y.,Guo, H.C.
Structural insights into the molecular ruler mechanism of the endoplasmic reticulum aminopeptidase ERAP1.
Sci Rep, 1:186-186, 2011

PubMed Abstract: Endoplasmic reticulum aminopeptidase 1 (ERAP1) is an essential component of the immune system, because it trims peptide precursors and generates the N--restricted epitopes. To examine ERAP1's unique properties of length- and sequence-dependent processing of antigen precursors, we report a 2.3 Å resolution complex structure of the ERAP1 regulatory domain. Our study reveals a binding conformation of ERAP1 to the carboxyl terminus of a peptide, and thus provides direct evidence for the molecular ruler mechanism.

PubMed: 22355701
DOI: 10.1038/srep00186

実験手法

X-RAY DIFFRACTION (2.3 Å)