Multiple iso-energetic-specific interactions involving the intrinsically-disordered region of sHSP HSPB1 define a quasi-ordered state, providing insights into inherited disease-associated mutations within the region that are thought to be disordered.
The C2-domain of cytoplasmic phospholipase A2α is structurally designed to target PC-rich membrane regions to increase the enzymatic efficiency of the catalytic domain, which prefers PCs with polyunsaturated acyl chains.
Aβ inhibitors effectively block its aggregation, while also reducing seeding of tau aggregation from Aβ, tau, and AD derived fibrils, suggesting the two share a structurally related disease relevant interface.
The METHYL-CpG-BINDING DOMAIN 7 (MBD7) complex promotes the activation (rather than repression) of transgenes that undergo DNA methylation and it does so without significantly altering their methylation status, placing this complex downstream of DNA methylation.
Structures of active and inactive conformations of a PP2C family phosphatase reveal a conserved switch that controls enzymatic activity and point to an unexpected relationship between phosphatases and proteasomal proteases.
Integrative structural analyses of human insulin degradingenzyme (IDE) reveal how IDE selectively degrades peptides that form toxicaggregates, which guides IDE-based therapeutic innovations to treat diabetesand Alzheimer's disease.