forthcoming articles

This study reports the co-crystallization of piperine with peroxisome proliferator-activated receptor gamma (PPARγ) ligand-binding domain, providing detailed insights into the piperine binding position and interactions with specific amino acids within the receptor. X-ray crystallographic analysis of the co-crystal structure revealed that piperine binds in the ligand-binding pocket of PPARγ via hydrogen-bonding and hydrophobic interactions, suggesting that it plays a role as a partial agonist or antagonist and thereby holds promise as a natural alternative to synthetic PPARγ modulators.

We report the structure of M. tuberculosis isoprenyl diphosphate synthase Rv2173 in three forms, including two with substrate (isoprenyl diphosphate and dimethylallyl diphosphate) occupying the allylic substrate site in different binding poses, with different numbers of metal ions bound. The homodimeric structures possess a canonical all-α-helical trans-isoprenyl diphosphate synthase fold, which supports small but significant differences, notably in the ordering of the C-terminus that closes the active site.

High-throughput protein crystallography is used at the heart of a pipeline to accelerate the discovery of bioactive natural products by capturing hits directly from unpurified biota samples using protein crystals.