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A new online GPCR structure analysis platform is presented and used to perform a comparative analysis of inactive/active state structures, resulting in detailed molecular mechanistic maps of activation of the major GPCR classes.
Structural studies of a positive allosteric modulator of the adenosine A1 receptor demonstrate the mechanisms by which stabilization of the GPCR–G protein complex bound to its endogenous agonist yields analgesic efficacy in an animal model of neuropathic pain.
An online and interactive G-protein coupled receptor (GPCR) structure analysis platform allows any researcher to analyze and visualize a plethora of structure–function relationships across the scales of atomic interactions to protein backbone rearrangements.
Comparative analysis of inactive/active-state structures reveals molecular mechanistic maps of activation of the major GPCR classes. The findings and new approaches lay the foundation for targeted receptor-function studies and drugs with desired modalities.
Dynamic changes in 2′-O-methylation of rRNA in human cells lead to ribosome heterogeneity and result in altered translation of select mRNAs, correlating with changes in cellular phenotypes.
Fluorescence imaging and fluorescence recovery after photobleaching assays reveal that the mitochondrial nucleoid forms a suborganelle via liquid–liquid phase separation interactions between mitochondrial DNA and the mitochondrial transcriptional machinery.
Biochemical, biophysical and structural analysis reveals how the scaffolding protein CcmM recruits the enzymes Rubisco and carbonic anhydrase into a condensate for encapsulation into carboxysomes—microcompartments in cyanobacteria that serve to optimize CO2 assimilation.
NMR visualization of phase-separated FUS and RNA polymerase II domains in models of transcriptional condensates show that a much wider array of residue types and interaction modes stabilize phases than previously proposed.
This study reveals the structural basis for the coupling specificity of one G-protein-coupled receptor, the β1-adrenergic receptor, to two different families of G proteins. Although the receptor adopts the same conformation, the G proteins have different interaction modes dictated by the overall structure.
Here the authors computationally test the hypothesis that RNA organizes the three-dimensional genome via a triplex-forming mechanism, providing evidence that lncRNA-targeted triplex hotspots can contribute to large-scale chromosome compartmentalization.