Tessera
Folgen

Dominika Borek

@dmborek.bsky.social

Scientist

16 Posts285 Follower917 Folgt
Ján Bíňovský@jbinovsky.bsky.social · last mo.

🔥My first (co)first-author paper is out🔥 The surfaces of Gram+ and Gram- bacteria are markedly different from each other. How are phages equipped to breach the Gram+ envelope❓ 💡We report a baseplate structure uniquely adapted to infect Gram+ S. aureus. A 🧵⬇️ 1/8 #phagesky #cryoEM 🧪

Bui Lab @McGill@builab.bsky.social · 2w ago

Interested in 3D-printed models of cryo-EM grids, autogrid and cryo-FIB for visual teaching/decoration. Download our model and print: makerworld.com/en/models/30... Designed in Blender by Khan Bao, an undergrad in the lab.

Cryo-EM Grids for Teaching - Free 3D Print Model - MakerWorld

Download this free 3D print file designed by CiliaBuilder. EM Grid Scaled ModelScaled up and simplified 3D model of EM grids and autogrids for demonstration of preparation process and milling. Content...

makerworld.com

Shicheng Guo@shihcheng.bsky.social · 2w ago

Explore new insights! Cryo-EM reveals how S961 and Ins-AC-S2 disrupt insulin signaling by binding the receptor's site 1 and site 2, unlike S597, which activates it. PMID:42265100, Nat Commun 2026, @NatureComms https://doi.org/10.1038/s41467-026-73851-1 #Medsky #Pharmsky #RNA #ASHG #ESHG 🧪

Structural basis of insulin receptor antagonism by bivalent site 1-site 2 ligands S961 and Ins-AC-S2 | Nature Communications

Congenital hyperinsulinism is a rare genetic disease characterized by overproduction of insulin. One class of potential treatments is insulin receptor antagonists like S961 and Ins-AC-S2, which comprise segments for binding each of the two insulin-binding sites (site 1 and site 2) on the receptor. Notably, S597 – containing the same receptor binding segments as S961 but in the opposite order (site 2-site 1) – is an insulin receptor agonist rather than an antagonist. Using cryo-EM, we show how both S961 and Ins-AC-S2 bind an inactive conformation of the receptor, thereby explaining their antagonism. Furthermore, our structures reveal how agonist vs. antagonist activity is influenced by the order of site 1- and site 2-binding modules in bivalent ligands. Additionally, we show subtle differences between the receptor-binding mechanisms of S961 and Ins-AC-S2, which include displacement or engagement of αCT, and a binding interface between the Ins-AC-S2 insulin and the receptor FnIII-2/inser

doi.org

Molecular Cell @cp-molcell.bsky.social · 2mo ago

Sub-2 Å cryo-EM structures of transcribing RNA polymerase II reveal critical roles of water molecules in catalysis

Sub-2 Å cryo-EM structures of transcribing RNA polymerase II reveal critical roles of water molecules in catalysis

The roles of water molecules in transcription have long been overlooked due to resolution limitations. Li et al. resolve high-resolution cryo-EM structures of RNA polymerase II and visualize previously undetected water molecules. These waters play essential roles in RNA polymerase II catalysis and in mediating interactions within the transcription machinery.

dlvr.it