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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.
Here the authors find that Polycomb repressive complex PRC1 functions independently of PRC2 to counteract Pol II binding, regulating transcription initiation and burst frequency.
A series of cryo-EM structures examining transcription initiation by vaccinia poxvirus RNA polymerase reveal how viral transcription factors identify and melt a promoter and how a polymerase-associated helicase mediates promoter escape.
Outer-arm dyneins (OADs) assemble in large arrays on the ciliary axoneme to drive rhythmic beating. Cryo-EM structures of microtubule-bound Tetrahymena thermophila OAD arrays reveal details of this complex assembly and suggest a model for its mechanism of coordinated action.
High-resolution cryo-EM structures of human ATM bound to ATPγS and two distinct ATM inhibitors provide insights into the mechanism of inhibitor selectivity and offer a framework for structure-based drug design.
Two de novo designed protein classes that link phosphorylation by tyrosine and serine kinases to protein-protein association provide potential new avenues to regulating cell function.
Human islet amyloid polypeptide (hIAPP) is a protein commonly forming aggregates in islet cells of those afflicted by type II diabetes. New structures of fibrils seeded with patient-derived material reveal a diverse repertoire of structures, some of which may resemble those appearing in vivo.
Cryo-EM structures of human type 1 and type 2 bradykinin receptors (B1R and B2R) reveal the basis for discrimination between the endogenous peptides des-Arg10-kallidin and bradykinin and their activation mechanism.
The cryo-EM structure of human mitochondrial RNase P bound to precursor tRNA reveals the molecular basis for the first step of RNA processing in human mitochondria.
The frameshift stimulation element (FSE) of coronaviruses is an RNA structure that is required for balanced expression of viral proteins and is thus a promising drug target. A structure of the SARS-CoV-2 FSE serves as a guide for the development of antisense oligonucleotides that impair virus replication.
Cryo-EM structures and functional analyses of the SARS-CoV-2 B.1.1.7 variant spike protein reveal that the A570D mutation creates a molecular switch to regulate up-down conformations of the ACE2 receptor-binding domain through a pedal-bin-like mechanism.
Cryo-EM structures of CRISPR–CasΦ, a small RNA-guided enzyme unique to bacteriophages, reveal how CasΦ binds to and cleaves DNA, paving the way for engineering of improved CasΦ variants for diagnostics and genome-editing applications.
Quantitative biochemical assays and high-resolution cryo-EM analysis reveal how the COVID-19 antiviral drug candidate molnupiravir causes lethal viral mutagenesis by the RNA-dependent RNA polymerase (RdRp) of SARS-CoV-2.
Identification of the tumor suppressor FLCN as an intracellular inhibitor of LDHA and a regulator of the Warburg effect provides a new paradigm for the regulation of glycolysis.
Crystallographic, electron microscopy and biophysical studies reveal how the synaptonemal complex component SYCE2-TEX12 undergoes self-assembly into fibrous supramolecular structures that mediate homologous chromosome synapsis in meiosis.
A crystal structure of the MEILB2–BRCA2 complex critical for BRCA2 recruitment to meiotic recombination sites shows the complex adopts a new 4:2 geometry that dictates the localization of both proteins in cells.
A cryo-EM structure of the active human melatonin receptor in complex with Gi reveals conformational changes upon activation and the molecular basis for G-protein selectivity.