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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.
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.
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.
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.
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.
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.
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.
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.
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.
The critical event in KRAS signaling and oncogenic transformation is activation of the RAF–MEK–MAPK cascade. This requires assembly of a multiprotein–lipid complex on the plasma membrane. In a tour de force of modeling, Mysore et al. now provide the first glimpse of what this structure may actually look like.
A structural model of a K-Ras nanocluster that promotes the stability and accessibility of active K-Ras and creates composite interfaces that facilitate Raf binding provides a framework to unravel MAPK signaling.
Cryo-EM and X-ray crystal structures reveal the architecture of the human Xkr8–Basigin complex, providing insights into the molecular mechanism of phospholipid scrambling.
PTEN is a key cell signaling lipid phosphatase that is regulated by C-terminal phosphorylation. Biophysical methods were used to illuminate the structural basis for PTEN regulation, which involves a dynamic N-terminal helix that influences catalysis.
Structures of the dephosphorylation complex for phosphorylated eIF2α reveal how contacts with the regulatory PPP1R15A subunit mediate substrate selectivity, providing a paradigm for dephosphorylation reactions by diverse combinatorially assembled holophosphatases.