Ontology highlight
ABSTRACT:
SUBMITTER: Nguyen TT
PROVIDER: S-EPMC3087843 | biostudies-literature | 2011 May
REPOSITORIES: biostudies-literature
Nguyen Tina T TT Chang Shih-Chung SC Evnouchidou Irini I York Ian A IA Zikos Christos C Rock Kenneth L KL Goldberg Alfred L AL Stratikos Efstratios E Stern Lawrence J LJ
Nature structural & molecular biology 20110410 5
ERAP1 trims antigen precursors to fit into MHC class I proteins. To fulfill this function, ERAP1 has unique substrate preferences, trimming long peptides but sparing shorter ones. To identify the structural basis for ERAP1's unusual properties, we determined the X-ray crystal structure of human ERAP1 bound to bestatin. The structure reveals an open conformation with a large interior compartment. An extended groove originating from the enzyme's catalytic center can accommodate long peptides and h ...[more]