Antigenic peptide trimming by ER aminopeptidases-Insights from structural studies

被引：43

作者：

Stratikos, Efstratios ^{[1
]}

Stern, Lawrence J. ^{[2
]}

机构：

[1] Natl Ctr Sci Res Demokritos, Athens 15310, Greece

[2] Univ Massachusetts, Sch Med, Dept Pathol, Worcester, MA 01655 USA

来源：

MOLECULAR IMMUNOLOGY | 2013年 / 55卷 / 3-4期

基金：

美国国家卫生研究院;

关键词：

Antigen processing; Structure; Mechanism; Enzyme; Peptide; Aminopeptidase; X-ray crystallography; Polymorphism; INSULIN-REGULATED AMINOPEPTIDASE; ENDOPLASMIC-RETICULUM AMINOPEPTIDASES; PSORIASIS SUSCEPTIBILITY LOCI; CLASS-I MOLECULES; CRYSTAL-STRUCTURE; ERAP1; POLYMORPHISM; SPECIFICITY; ASSOCIATION; PRECURSORS;

D O I：

10.1016/j.molimm.2013.03.002

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Generation and destruction of antigenic peptides by ER resident aminopeptidases ERAP1 and ERAP2 have been shown in the last few years to be important for the correct functioning and regulation of the adaptive immune response. These two highly homologous aminopeptidases appear to have evolved complex mechanisms well suited for their biological role in antigen presentation. Furthermore, polymorphic variability in these enzymes appears to affect their function and predispose individuals to disease. This review discusses our current understanding of the molecular mechanisms behind ERAP1/2 function as suggested by several recently determined crystallographic structures of these enzymes. (c) 2013 Elsevier Ltd. All rights reserved.

引用

页码：212 / 219

页数：8

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