Structural highlights
Publication Abstract from PubMed
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 A 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.
Structural insights into the molecular ruler mechanism of the endoplasmic reticulum aminopeptidase ERAP1.,Gandhi A, Lakshminarasimhan D, Sun Y, Guo HC Sci Rep. 2011;1:186. Epub 2011 Dec 13. PMID:22355701[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gandhi A, Lakshminarasimhan D, Sun Y, Guo HC. Structural insights into the molecular ruler mechanism of the endoplasmic reticulum aminopeptidase ERAP1. Sci Rep. 2011;1:186. Epub 2011 Dec 13. PMID:22355701 doi:10.1038/srep00186
