Nature Structural Biology

Most recent issue of Nature Structural Biology

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  • doi:10.1038/s41594-018-0030-z

    2′-O-methylation within mRNA coding regions sterically perturbs interactions of ribosomal-monitoring bases with cognate codon–anticodon helices, leading to excessive rejection of cognate aminoacylated tRNAs during initial selection and proofreading.' );return false" > 2′-O-methylation in mRNA disrupts tRNA decoding during translation elongation
  • doi:10.1038/s41594-018-0031-y

    Crystal structures of human GPT in complex with tunicamycin provide insight into mechanisms of inhibition and differences between human and bacterial enzymes, leading to the design of an analog with specificity for the bacterial enzyme.' );return false" > GlcNAc-1-P-transferase–tunicamycin complex structure reveals basis for inhibition of N-glycosylation
  • doi:10.1038/s41594-018-0029-5

    In vivo, in vitro and in silico experiments demonstrate that interface residues of homomeric proteins are enriched toward protein C termini to avoid premature assembly and aggregation.' );return false" > Cotranslational protein assembly imposes evolutionary constraints on homomeric proteins
  • doi:10.1038/s41594-018-0028-6

    Yeast surface display platform allows nanobody discovery within two to three weeks. Examples include nanobodies for crystallographic applications, targeting nonpurified antigen or conformationally selective nanobodies to two distinct human GPCRs.' );return false" > Yeast surface display platform for rapid discovery of conformationally selective nanobodies
  • doi:10.1038/s41594-018-0027-7

    Cryo-ET analyses of the microtubule-bound mouse dynein–dynactin complex reveal two dimeric dyneins interacting with the dynactin–cargo adaptor complex, a configuration that can account for processivity and directionality of dynein transport activity.' );return false" > Cryo-electron tomography reveals that dynactin recruits a team of dyneins for processive motility
  • doi:10.1038/s41594-018-0025-9

    Wu and Wilson review our structural knowledge of influenza virus HA and broadly neutralizing antibodies, which have opened the way for design of novel vaccines and therapeutics.' );return false" > Structural insights into the design of novel anti-influenza therapies
  • doi:10.1038/s41594-018-0026-8

    The X-ray structures of engineered variants of the human serotonin transporter show that the antidepressants sertraline, fluvoxamine and paroxetine occupy the central substrate-binding site and stabilize the transporter in an outward-open conformation.' );return false" > Structural basis for recognition of diverse antidepressants by the human serotonin transporter
  • doi:10.1038/s41594-018-0023-y

    Cryo-EM analyses of human PRC2 bound to dinucleosomes with one unmodified (substrate) and one H3K27me3-containing (activating) nucleosome support a model for H3K27me3-based PRC2 activation and spreading.' );return false" > Cryo-EM structures of PRC2 simultaneously engaged with two functionally distinct nucleosomes
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