Ontology highlight
ABSTRACT:
SUBMITTER: Wang L
PROVIDER: S-EPMC2475331 | biostudies-literature | 2008 Jul
REPOSITORIES: biostudies-literature
Wang Likun L Wang Lei L Vavassori Stefano S Li Shengjian S Ke Huimin H Anelli Tiziana T Degano Massimo M Ronzoni Riccardo R Sitia Roberto R Sun Fei F Wang Chih-Chen CC
EMBO reports 20080613 7
ERp44 mediates thiol-dependent retention in the early secretory pathway, forming mixed disulphides with substrate proteins through its conserved CRFS motif. Here, we present its crystal structure at a resolution of 2.6 A. Three thioredoxin domains-a, b and b'-are arranged in a clover-like structure. A flexible carboxy-terminal tail turns back to the b' and a domains, shielding a hydrophobic pocket in domain b' and a hydrophobic patch around the CRFS motif in domain a. Mutational and functional s ...[more]