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Evnouchidou, I., Momburg, F., Papakyriakou, A., Chroni, A., Leondiadis, L., Chang, S.C., and Stratikos, E. (2008) The Internal Sequence of the Peptide-Substrate Determines Its N-Terminus Trimming by ERAP1. PLoS ONE, 3, e3658-e3658.
http://dx.doi.org/10.1371/journal.pone.0003658

has been cited by the following article:

• TITLE: Single-Chain Expression and Crystallization of an Antigenic C-Terminus in Complex with the Regulatory Domain of ER Aminopeptidase 1

  AUTHORS: Lufei Sui, Amit Gandhi, Hwai-Chen Guo

  KEYWORDS: Endoplasmic Reticulum Aminopeptidase 1 (ERAP1), ERAP1 Regulatory Domain, Antigen Presentation, X-Ray Crystallography

  JOURNAL NAME: Crystal Structure Theory and Applications, Vol.4 No.4, November 24, 2015

  ABSTRACT: Human endoplasmic reticulum aminopeptidase 1 (ERAP1) is one of two ER luminal aminopeptidases that participate in the final processing of peptide precursors and generates the N-termini of the MHC class I-restricted epitopes. In order to investigate the interactions of its binding site with substrate peptides, X-ray crystallographic analyses have been carried out to study structures of ERAP1 regulatory (ERAP1_R) domain in complex with antigenic peptides. Single-chain bimodular constructs with various antigenic peptides linked to the C-terminal end of ERAP1_R domain are designed to facilitate crystallization process of these complexes. These recombinant proteins have been purified and crystalized, and x-ray diffraction data of one crystal have been processed to a resolution of 2.8 . The crystal belongs to the space group P21, with unit cell parameters a =64.2, b = 66.8, c = 66.3 , β = 110.2°. A Refmac-refined omit map reveals a clear density for the antigenic peptide’s carboxylate-end that is in contact with the ERAP1 regulatory domain of neighboring molecule. Thus the single-chain bimodular constructs have provided an expedited approach to study sequence-specific interactions between the ERAP1 regulatory domain and antigen peptide’s C-terminal ends.