18 research outputs found
Production of flavor esters catalyzed by lipase B from Candida antarctica immobilized on magnetic nanoparticles
Reevaluation of the PPAR-beta/delta Ligand Binding Domain Model Reveals Why It Exhibits the Activated Form.
Evaluation of the topoisomerase II-inactive bisdioxopiperazine ICRF-161 as a protectant against doxorubicin-induced cardiomyopathy
Recombinant human PPAR-beta/delta ligand-binding domain is locked in an activated conformation by endogenous fatty acids
High-resolution crystallographic structures of recombinant human peroxisome proliferator-activated receptor ligand-binding domain (isotype beta/delta) reveal a fatty acid in the binding site. Mass spectrometry confirmed the presence of C16:0, C16:1, C18:0 and C18:1 in a ratio of approximately 3:2:1:4 with 11, Z-octadecenoic acid (cis-vaccenic acid) identified as the predominant species. These are endogenous fatty acids acquired from the bacterial expression system, and serve to lock the ligand-binding domain into the activated conformation. A requirement for crystal growth, the additive n-heptyl-beta-(D)-glucopyranoside, binds near the activation function helix where recognition of co-activator proteins occurs. Our observations suggest potential physiological ligands for human PPAR-beta/delta and highlight that reported binding studies must be treated with caution unless endogenous fatty acids have been removed from the sample prior to analysis. (c) 2005 Elsevier Ltd. All rights reserved.</p