title: Structural insights into the molecular ruler mechanism of the endoplasmic reticulum aminopeptidase ERAP1.
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.
authors.affiliation: Department of Biological Sciences, University of Massachusetts Lowell, 1 University Avenue, Lowell, MA 01854, USA.
authors.forename: Amit
authors.initials: A
authors.lastname: Gandhi
authors.forename: Damodharan
authors.initials: D
authors.lastname: Lakshminarasimhan
authors.forename: Yixin
authors.initials: Y
authors.lastname: Sun
authors.forename: Hwai-Chen
authors.initials: HC
authors.lastname: Guo
mesh_terms: D000495:Allosteric Site; D000626:Aminopeptidases / Q000737:chemistry* / Q000502:physiology*; D017951:Antigen Presentation; D000941:Antigens / Q000737:chemistry; D001665:Binding Sites; D004721:Endoplasmic Reticulum / Q000378:metabolism; D000939:Epitopes / Q000737:chemistry; D006639:Histidine / Q000737:chemistry; D015395:Histocompatibility Antigens Class I / Q000737:chemistry; D006801:Humans; D015778:Minor Histocompatibility Antigens; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry; D011485:Protein Binding; D017434:Protein Structure, Tertiary
chemical_list: D000941:Antigens; D000939:Epitopes; D015395:Histocompatibility Antigens Class I; D015778:Minor Histocompatibility Antigens; D010455:Peptides; D006639:Histidine; D000626:Aminopeptidases; C464841:ERAP1 protein, human