Related Experiment Video
Updated: May 24, 2026

Visualization of Endoplasmic Reticulum Localized mRNAs in Mammalian Cells
Published on: December 17, 2012
Structural insights into the molecular ruler mechanism of the endoplasmic reticulum aminopeptidase ERAP1
Amit Gandhi1, Damodharan Lakshminarasimhan, Yixin Sun
1Department of Biological Sciences, University of Massachusetts Lowell, 1 University Avenue, Lowell, MA 01854, USA.
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.
More Related Videos
Related Concept Videos
Directing Proteins to the Rough Endoplasmic Reticulum
Regulation of the Unfolded Protein Response
Tail-anchoring of Proteins in the ER Membrane
Export of Misfolded Proteins out of the ER
The Endoplasmic Reticulum
Protein Modifications in the RER
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.

