Department of Biological Sciences, University of Massachusetts Lowell, 1 University Avenue, Lowell, MA 01854, USA.
Sci Rep. 2011;1:186. doi: 10.1038/srep00186. Epub 2011 Dec 13.
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.
内质网氨肽酶 1(ERAP1)是免疫系统的重要组成部分,因为它能修剪肽前体并产生 N-限制表位。为了研究 ERAP1 对抗原前体的长度和序列依赖性加工的独特特性,我们报告了 ERAP1 调节域的 2.3Å 分辨率复合物结构。我们的研究揭示了 ERAP1 与肽羧基末端的结合构象,从而为分子标尺机制提供了直接证据。