Crystal structure of Plasmodium vivax macrophage migration inhibitory factor

The production, crystallization and 1.8 Å resolution crystal structure of macrophage migratory inhibitory factor from P. vivax are reported.

Structural insights into the binding mode of the hypnotic drug vornorexant to orexin receptors

The crystal structure of the human orexin type 2 receptor–vornorexant complex (3.29 Å resolution) and orexin type 1 receptor docking revealed a conserved U-shaped binding conformation, explaining the high affinity and balanced dual antagonism of this dual orexin receptor antagonist. The structural data validate the rational design that incorporated a 1,3-oxazinan ring and pyrazole moiety to reduce lipophilicity while maintaining strong receptor affinity, highlighting the potential of vornorexant as an effective insomnia treatment with a lower risk of next-day residual effects.

Crystal structure of the plant GABA aminotransferase AtGABA-T from Arabidopsis thaliana

The crystal structure of A. thaliana γ-aminobutyric acid aminotransferase (GABA-T) reveals that plant GABA-T belongs to the class III aminotransferase family and employs a C-terminal arginine residue for γ-aminobutyric acid recognition, in contrast to the N-terminal arginine used by class II enzymes.

Crystal structures of PCNA1 and PCNA2 from Aeropyrum pernix: implications for a distorted heterotrimeric sliding clamp

Crystal structures of A. pernix PCNA1 (1.60 Å resolution) and PCNA2 (2.17 Å resolution) are reported. High-resolution analysis reveals a rare nonproline cis-peptide bond in PCNA1 that may cause steric hindrance at the subunit interface, suggesting a distorted or symmetry-broken heterotrimeric PCNA ring.

Structural analysis of the flexibility of the Ubl2 domain within the papain-like protease of SARS-CoV-2

The ubiquitin-like domain 2 (Ubl2) of the SARS-CoV-2 virus is necessary for the stability and catalytic efficiency of its papain-like protease (PLpro). Our crystallographic study reveals that the Ubl2 domain exhibits notable flexibility and can adopt a conformation that places itself away from the PLpro catalytic domain, representing a new conformation from those reported so far for SARS-CoV-1 or SARS-CoV-2. The structural flexibility of Ubl2 could be allosterically related to the stability of the zinc-finger domain.