Helix Biostructures

30/10/2026

One small receptor can have a surprisingly big influence on appetite, energy balance, and mood. Neuropeptide Y receptors control several important physiological processes and are attractive drug targets, but Y5R has remained structurally elusive. This study reports one 2.9 Å cryo-EM structure of NPY bound to Y5R and Gi1, revealing how the peptide sits in the receptor and what drives subtype selectivity ( https://doi.org/10.1002/anie.4104254 ). Surprisingly, changing Y407 reduced receptor activation by more than 180-fold without affecting NPY binding, separating recognition from signaling. These insights provide a structural foundation for designing more selective ligands and open the door to targeting Y5R more effectively in drug discovery. The article is open access and well worth reading for anyone interested in where Y5R drug discovery may go next!

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16/10/2026

HIV-1 gets most of the attention, but HIV-2 has evolved its own way of outsmarting our antiviral defenses. Understanding HIV-2 matters because its biology and treatment options differ from HIV-1. This study produced two cryo-EM reconstructions of the HIV-2 Vif-A3H-CBFβ complex, capturing dimeric and monomer-focused views ( https://loom.ly/rysq93s ). The structures show how dsRNA brings two A3H molecules together and how Vif and CBFβ help target them for destruction. Surprisingly, HIV-2 Vif binds A3H through a completely different interface from HIV-1 Vif, even though both disable the same antiviral protein. The full paper is freely available, making it a good one to dive into yourself. Happy reading!

Did you know... Helix’s deep expertise in cryo-EM and protein crystallography shortens timelines and strengthens confidence across R&D programs? Let’s power your science forward together! https://loom.ly/DlFJ3Ss

23/09/2026

What if an antibiotic could work again simply by blocking the pump that ejects it? Antibiotic resistance remains a challenge, and efflux pumps are difficult drug targets. This study identified IMP-2380, a NorA efflux pump inhibitor that restores ciprofloxacin activity against MRSA ( https://loom.ly/tHOksk0 ). One cryo-EM structure (2.52 Å) showed IMP-2380 locking NorA in an outward-open state and blocking antibiotic efflux. Curiously, a screen designed to find SOS-response inhibitors instead uncovered NorA as the key target. Even more striking, the inhibitor binds from outside the cell, avoiding the need to cross the bacterial membrane. Cool stuff! The article is open access and certainly worth reading!

Did you know... Cryo-EM is transforming structure-based drug design? Get atomic-level insights into your targets, mechanisms, and interactions with our expertise. Let’s collaborate and contact us today! https://loom.ly/KNHs0P4

15/09/2026

What happens when we look beyond the “classic” NMDA receptors? Most structural studies of NMDA receptors have focused on canonical GluN1–GluN2 complexes, while GluN3A-containing receptors remain less understood despite growing pharmacological interest. This study ( https://loom.ly/bhwvP4U ) captured four cryo-EM structures spanning antagonist-bound, preactive, active, and desensitized states. The structures show how glycine-driven GluN3A movements open the channel and how the receptor shifts during desensitization. Surprisingly, the GluN1 antagonist CGP-78608 actually boosts activity by preventing GluN3A from rotating into the desensitized state. The study also reveals two-fold symmetric channel opening, unlike related receptors. The article is open access and a great read!

Did you know... Helix offers industry-leading cryo-EM, crystallography and structure analysis services tailored to complex biological systems? We bring unmatched precision to your most challenging projects. Let’s explore how we can support your next breakthrough! https://loom.ly/_ss_hRE

31/08/2026

Obtaining protein complexes in both resting and activated states is especially valuable because it reveals activation-linked structural changes, although flexible and dynamic regions can remain difficult to resolve. This review (https://doi.org/10.1038/s41423-026-01447-2) highlights how cryo-EM has transformed NADPH oxidase biology, including resting and activated NOX2-p22phox structures, calcium-driven NOX5 rearrangements, and integration with AlphaFold and molecular dynamics. These advances connect NOX architecture to immunity, metabolism, pollution, fibrosis, cancer, and drug design. Interestingly, cryo-EM revealed how NOX5 undergoes conformational changes when interacting with calcium. The review is open access and well worth exploring the fascinating world of redox signaling. Enjoy!

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27/08/2026

Intracellular pH is easy to overlook, and a small shift in cellular pH may have a surprisingly big impact on how neurons behave. Using cryo-EM, this study captured NBCn2 in three states and uncovered an unusual binding arrangement involving two sodium ions and one carbonate ion ( https://loom.ly/1KJbkAE ). Structure-guided screening also identified Cmpd38J, which reduced neuronal activity in cultured cells and brain slices. Surprisingly, knocking down NBCn2 alone did not reduce firing because related transporters appear to compensate. All this makes NBCn2 an intriguing target for neurological diseases. The article is freely available making it an easy one to explore for a closer look at these findings. Enjoy!

Did you know... Whether you are working with wild-type, mutant, or engineered proteins, our structural biology platform provides the resolution you need? Let’s talk about unlocking your next discovery! https://loom.ly/inhKYLo

11/08/2026

30/07/2026

What if one bacterial enzyme can grab two tRNAs at the same time? That is exactly what this study uncovered. Using cryo-EM, the authors solved the structure of E. coli TGT, an enzyme closely related to the Shigella version involved in virulence. The biggest surprise was that the enzyme dimer can bind and modify two tRNAs simultaneously, overturning the long-standing one-tRNA model ( https://loom.ly/ToZB5f0 ). The structures also revealed key contacts outside the active site and inspired stronger dual-hairpin RNA substrates. These insights could support new antivirulence therapies and improved RNA-labeling tools. The full open-access article is free to read, and this one is worth opening for the structural surprise alone!

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