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A 20S proteasome complex localizes to the neuronal plasma membrane, where it produces and releases extracellular peptides that induce neuronal signalling. Cover image from LuisPortugal /E+/Getty. (p 419)
Separases are crucial cell cycle proteases that control the metaphase-to-anaphase transition by cleaving chromosomal cohesin rings. Two new high-resolution structures of separase bound by its inhibitory chaperone securin illustrate intriguing regulatory mechanisms.
The binding of foreign peptides to host major histocompatibility complex (MHC) forms the basis of adaptive immune recognition. The MHC and T cell receptors (TCRs) use diverse structural solutions to enhance peptide presentation and recognition, and two new reports provide insights into noncanonical modes of detection and binding.
Chromatin-remodeling enzymes perform the formidable task of reorganizing the structure of a stable macromolecular assembly, the nucleosome. Recently published work demonstrates that the SNF2H chromatin remodeler distorts the histone octamer structure upon binding to the nucleosome, then taps into this induced plasticity to productively achieve nucleosome sliding.
TOP2 collaborates with the BAF complex genome-wide to form and resolve facultative heterochromatin at transcriptional regulatory elements recognized by pluripotency factors.
Capture Hi-C analysis reveals that DNA double-strand breaks within transcriptionally active regions of the human genome form clusters that exhibit delayed repair in the G1 phase of the cell cycle.
Human OGA forms an unusual arm-in-arm homodimer with a substrate-binding cleft that affords extensive interactions with the peptide substrate in a recognition mode distinct from that of its bacterial homologs.
Cryo-EM analyses of the initial contact of the HIV-1 Env trimer with the CD4 receptor reveal that CD4 interacts with two gp120 protomers; these quaternary contacts are important for viral infectivity.
HIV Tat binding to the exterior of Aβ fibrils induces lateral aggregation and formation of fibers with increased adhesion, rigidity and mechanical resistance, thus potentially accounting for their higher neurotoxicity.
Structural determination and analysis of HLA-I that presents an HIV-derived peptide to an NK cell receptor reveal that N-terminal extended epitope conformations contribute to immune recognition and mechanisms of HIV immune escape.
Crystal structure analysis combined with sequencing approaches uncover a broad T cell receptor repertoire and reveal the structural basis of influenza M1 epitope recognition.
The interaction of Hsp90 with misfolded monomeric transthyretin is characterized via biophysical approaches, and the data indicate that Hsp90 may have a distinct recognition mode for aggregation-prone proteins.
Cryo-EM analyses provide a near-atomic view of the C. elegans securin–separase complex, with insights into the mechanism by which securin inhibits separase's protease activity.
A 20S proteasome complex localizes to neuronal plasma membrane, where it produces and releases extracellular peptides that induce neuronal calcium signaling.
