Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain
the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in
Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles
and JavaScript.
Cryo-EM and tomography imaging of influenza virus fusion with target membranes reveal structural intermediates of HA surface glycoprotein and their interactions with membranes as well as ultrastructural changes in the virus that accompany membrane fusion.
Analyses in supported lipid bilayers and in cells shed light on the roles of multiple SOS-membrane interactions in SOS's membrane recruitment and association, processive activation of Ras and signal attenuation.
An interactive structure-based approach was used to improve a vaccine antigen against respiratory syncytium virus (RSV), thus leading to immunogens with higher stability that elicit higher neutralizing titers in mice.
A cryo-EM structure of yeast AAA+ protein disaggregase Hsp104 with AMP-PNP reveals a spiral arrangement of the protomers and a continuous path for polypeptide translocation that explains Hsp104's processivity mechanism during disaggregation.
The inability of A-form RNA to form Hoogsteen base pairs provides a mechanism for how post-transcriptional modifications can disrupt RNA structure and might help explain why DNA is the molecular choice for storing genetic information.
Light-scattering kinetics and atomic force and electron microscopy analyses show that Hsp70-mediated disassembly of clathrin cages occurs via a collision-pressure mechanism consistent with the entropic pulling model.
The eukaryotic Elongator complex participates in modification of uridines in tRNAs. Structural and functional work on a bacterial Elp3, the catalytic subunit of Elongator, provides insight into the function and mechanism of this important enzyme.
Mass spectrometry, kinetics studies and in silico analyses indicate that multiple copies of the Skp chaperone are required for sequestration of 16-stranded or larger OMPs and prevention of their aggregation.
A cryo-EM structure of the human 26S proteasome in a resting state at an average resolution of 3.5 Å reveals details in the interactions between subunits. An additional structure of the proteasome with USP14 bound suggests a mechanism for its activation.
Structural and functional analysis of the Swi2/Snf2 remodeler demonstrates that the catalytic core of the protein is a competent remodeling machine, which rests in an inactive conformation poised for activation.
EPR spectroscopy analyses elucidate how lipids affect the conformational dynamics of a multidrug secondary transporter, LmrP, and indicate a key role of the lipid headgroups in shaping the conformational-energy landscape of the transporter.
Solid-state NMR analyses reveal that the free backbone carbonyl groups associated with proline residues in the transmembrane helices play a key role in mediating rhodopsin activation.
The crystal structure of the putative exonuclease Exuperantia, required for Drosophila anterior patterning, reveals an EXO-SAM-like domain architecture that is catalytically inactive but mediates dimerization and RNA binding, which are essential for bicoid localization.
A new study reveals that 53BP1 influences high-fidelity homology-directed repair by showing that its depletion in the presence of increasing DNA-damage levels triggers a shift from RAD51-dependent gene conversion, an error-free process, to RAD52-mediated single-strand annealing, which is mutagenic.
Biochemical, structural and cell-based analyses reveal a chaperone-like function of glycyl-tRNA synthetase, which supports neddylation via direct interactions with NEDD8, E1 and E2.
BoNT/A1 invades motoneurons by binding to the neuronal receptor SV2. A combination of structural, biophysical and cellular analyses reveal that BoNT/A1 binding and uptake require glycosylation of SV2.
The histone methyltransferase DOT1L and the chromatin reader BRD4 together facilitate transcription of genes critical to the molecular pathogenesis of MLL leukemia.
A new 'metal mimic' mutagenesis approach that captures a T5 flap endonuclease complex with an intact DNA substrate provides structural evidence that the single-stranded 5′ flap generated by Okazaki-fragment synthesis threads through the flap endonuclease enzyme.
The canonical transcription factor ERG promotes degradation of a subset of mRNAs linked to mitotic progression by recruiting the CCR4–NOT deadenylation complex, thus revealing a new regulatory interplay between mRNA synthesis and degradation.
The E3 ubiquitin ligase activity of the BRCA1–BARD1 complex is required to reposition 53BP1 on damaged chromatin and to promote DNA resection and repair via homologous recombination, in a mechanism involving the chromatin remodeler SMARCAD1.