3RJO

Crystal Structure of ERAP1 Peptide Binding Domain

Summary for 3RJO

• Entry DOI: 10.2210/pdb3rjo/pdb
• Descriptor: Endoplasmic reticulum aminopeptidase 1, 1,2-ETHANEDIOL (3 entities in total)
• Functional Keywords: erap1, aminopeptidase, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Endoplasmic reticulum membrane; Single-pass type II membrane protein (Probable): Q9NZ08
• Total number of polymer chains: 1
• Total formula weight: 48839.88

Authors

Guo, H.-C.,Lakshminarasimhan, D.,Gandhi, A. (deposition date: 2011-04-15, release date: 2011-12-21, Last modification date: 2024-11-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.3 Å)