Structure of the substrate-binding b' domain of the Protein Disulfide Isomerase-Like protein of the Testis.

ABSTRACT: Protein Disulfide Isomerase-Like protein of the Testis (PDILT) is a testis-specific member of the PDI family. PDILT displays similar domain architecture to PDIA1, the founding member of this protein family, but lacks catalytic cysteines needed for oxidoreduction reactions. This suggests special importance of chaperone activity of PDILT, but how it recognizes misfolded protein substrates is unknown. Here, we report the high-resolution crystal structure of the b' domain of human PDILT. The structure reveals a conserved hydrophobic pocket, which is likely a principal substrate-binding site in PDILT. In the crystal, this pocket is occupied by side chains of tyrosine and tryptophan residues from another PDILT molecule, suggesting a preference for binding exposed aromatic residues in protein sub

SUBMITTER: Bastos-Aristizabal S 

PROVIDER: S-EPMC4894388 | biostudies-literature | 2014 Mar

REPOSITORIES: biostudies-literature