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Current opinion in structural biology最新文献

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Beyond resolution: Cryo-electron tomography of microbial nanomachines in native host context. 超越分辨率：微生物纳米机器在原生宿主环境下的低温电子断层扫描。
IF 6.1 2区 生物学
Current opinion in structural biology Pub Date : 2026-05-07 DOI: 10.1016/j.sbi.2026.103280
Bas Leemburg, Mohamad Harastani, Armel Bezault, Ariane Briegel
{"title":"Beyond resolution: Cryo-electron tomography of microbial nanomachines in native host context.","authors":"Bas Leemburg, Mohamad Harastani, Armel Bezault, Ariane Briegel","doi":"10.1016/j.sbi.2026.103280","DOIUrl":"https://doi.org/10.1016/j.sbi.2026.103280","url":null,"abstract":"<p><p>Cryo-electron tomography (cryo-ET) has revolutionized visualization of bacterial nanomachines by revealing molecular structures in situ under near-native conditions. This review highlights recent advances extending cryo-ET from isolated cells to host-microbe interactions within intact tissues. We discuss technical solutions for large-volume imaging such as cryo-focused ion beam milling, correlative light and electron microscopy, and serial lift-out workflows that preserve native structural context. Computational developments in AI-driven denoising, segmentation, and sub-tomogram averaging enhance interpretability of low-dose tomograms. Using examples from predatory bacteria, intracellular pathogens, and squid symbionts, we demonstrate how cryo-ET elucidates mechanistic details of microbial interactions.</p>","PeriodicalId":10887,"journal":{"name":"Current opinion in structural biology","volume":"98 ","pages":"103280"},"PeriodicalIF":6.1,"publicationDate":"2026-05-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147856141","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
The twisted tale of cotranslational protein complex assembly. 协同翻译蛋白复合物组装的扭曲故事。
IF 6.1 2区 生物学
Current opinion in structural biology Pub Date : 2026-05-07 DOI: 10.1016/j.sbi.2026.103281
Saurav Mallik, Ayala Shiber
{"title":"The twisted tale of cotranslational protein complex assembly.","authors":"Saurav Mallik, Ayala Shiber","doi":"10.1016/j.sbi.2026.103281","DOIUrl":"https://doi.org/10.1016/j.sbi.2026.103281","url":null,"abstract":"<p><p>Macromolecular complexes are cells' functional units, and their correct and efficient assembly is critical to life's processes. Complex assembly was classically described as the encounter of fully synthesized, mature protein subunits, yet an amalgam of current studies shows that cotranslational assembly is prevalent, in which nascent proteins vectorially form interfaces with their partners during translation. In this review, we examine the advances in this emerging field. We discuss the thermodynamic and kinetic principles underlying different modes of assembly and highlight how the specific structural/biophysical features of the corresponding complexes enable them. We propose that cotranslational assembly produces kinetically stable oligomeric states that resist dissociation and stochastic conformational changes, thereby conferring functionality amid molecular crowding or environmental stresses.</p>","PeriodicalId":10887,"journal":{"name":"Current opinion in structural biology","volume":"98 ","pages":"103281"},"PeriodicalIF":6.1,"publicationDate":"2026-05-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147856174","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Three-color single-molecule fluorescence resonance energy transfer to study macromolecular dynamics. 三色单分子荧光共振能量转移研究大分子动力学。
IF 6.1 2区 生物学
Current opinion in structural biology Pub Date : 2026-05-06 DOI: 10.1016/j.sbi.2026.103278
Jia Gao, Bo Yuan, Sourav Mondal, Rajib Basak, Tae-Hee Lee
{"title":"Three-color single-molecule fluorescence resonance energy transfer to study macromolecular dynamics.","authors":"Jia Gao, Bo Yuan, Sourav Mondal, Rajib Basak, Tae-Hee Lee","doi":"10.1016/j.sbi.2026.103278","DOIUrl":"https://doi.org/10.1016/j.sbi.2026.103278","url":null,"abstract":"<p><p>Single-molecule fluorescence resonance energy transfer (smFRET) is a powerful tool to probe macromolecular dynamics. Two-color smFRET, however, provides only one-dimensional distance information, limiting its use in complex systems. Multicolor smFRET with three or more fluorophores can overcome this, though three is often the practical limit due to the narrow selection of dyes with suitable spectral properties, the challenges of labeling with multiple fluorophores, and the complexity of data interpretation. Here, we survey recent investigations of the dynamics of macromolecules and their complexes based on three-color smFRET. In this review, three-color smFRET refers to the use of three fluorophores in a FRET system where two or all three fluorophores may participate in FRET at a given time point. We aim to highlight structural biology problems particularly well suited for three-color smFRET and to provide a brief overview of designing and implementing such experiments in light of their benefits and challenges.</p>","PeriodicalId":10887,"journal":{"name":"Current opinion in structural biology","volume":"98 ","pages":"103278"},"PeriodicalIF":6.1,"publicationDate":"2026-05-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147834710","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Control of viral envelope glycoprotein function revealed by single-molecule imaging. 单分子成像揭示病毒包膜糖蛋白功能的控制。
IF 6.1 2区 生物学
Current opinion in structural biology Pub Date : 2026-05-06 DOI: 10.1016/j.sbi.2026.103275
Matthew Unger, James B Munro
{"title":"Control of viral envelope glycoprotein function revealed by single-molecule imaging.","authors":"Matthew Unger, James B Munro","doi":"10.1016/j.sbi.2026.103275","DOIUrl":"https://doi.org/10.1016/j.sbi.2026.103275","url":null,"abstract":"<p><p>Viral envelope glycoproteins catalyze membrane fusion during entry into cells. Envelope glycoprotein function has traditionally been viewed through the lens of kinetic control, where environmental cues like pH trigger irreversible refolding from the pre-fusion conformation to the post-fusion conformation. Single-molecule Förster resonance energy transfer (smFRET) imaging has revealed an additional layer of thermodynamic control that governs the conformational dynamics of envelope glycoproteins in their pre-fusion form. smFRET studies of the envelope glycoproteins from HIV-1, SARS-CoV-2, MERS-CoV, Ebola virus, and influenza A virus demonstrate that these glycoproteins dynamically sample an ensemble of pre-fusion conformations whose relative stabilities respond to pH, receptor binding, ions, and host proteases. This thermodynamic tuning precedes the kinetically controlled transition that promotes membrane fusion. Collectively, smFRET imaging has transformed our understanding of viral entry, illustrating how the pre-fusion energy landscape of envelope glycoproteins is tuned by the host environment to maintain viral fitness.</p>","PeriodicalId":10887,"journal":{"name":"Current opinion in structural biology","volume":"98 ","pages":"103275"},"PeriodicalIF":6.1,"publicationDate":"2026-05-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147834683","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Transformers as a substrate for structural biology 变压器作为结构生物学的基质。
IF 6.1 2区 生物学
Current opinion in structural biology Pub Date : 2026-04-01 Epub Date: 2026-02-06 DOI: 10.1016/j.sbi.2025.103218
Ashar J. Malik , Stephanie Portelli , David B. Ascher
{"title":"Transformers as a substrate for structural biology","authors":"Ashar J. Malik ,&nbsp;Stephanie Portelli ,&nbsp;David B. Ascher","doi":"10.1016/j.sbi.2025.103218","DOIUrl":"10.1016/j.sbi.2025.103218","url":null,"abstract":"<div><div>Transformers are rapidly reshaping structural biology. We argue the reason is “Emergent Latent Biology” (ELB): transformers place proteins into high-dimensional representations where hidden biophysical patterns become easier to see. We explore this concept across four key areas: protein folding, variant effects, protein–protein and protein–drug interactions. Highlighting recent gains, we note that traditional, physics-based calculations are still required for the hardest quantitative jobs, like predicting precise binding strength. Furthermore, we draw attention to major pitfalls, arguing progress depends on solving the critical “chemistry gap,” modelling chemical modifications, and the “dynamics gap”, predicting protein movement, which requires better validation methods and new large-scale experiments.</div></div>","PeriodicalId":10887,"journal":{"name":"Current opinion in structural biology","volume":"97 ","pages":"Article 103218"},"PeriodicalIF":6.1,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146137351","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Why are there no clinically-approved drugs targeting disordered proteins? 为什么没有临床批准的针对无序蛋白质的药物？
IF 6.1 2区 生物学
Current opinion in structural biology Pub Date : 2026-04-01 Epub Date: 2026-03-02 DOI: 10.1016/j.sbi.2026.103236
Thomas Löhr , Gogulan Karunanithy , Gabriella T. Heller
{"title":"Why are there no clinically-approved drugs targeting disordered proteins?","authors":"Thomas Löhr ,&nbsp;Gogulan Karunanithy ,&nbsp;Gabriella T. Heller","doi":"10.1016/j.sbi.2026.103236","DOIUrl":"10.1016/j.sbi.2026.103236","url":null,"abstract":"<div><div>Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) are critical regulators in health and disease but remain underexploited as drug targets. Unlike folded proteins, they populate dynamic ensembles where interactions can be transient or multivalent, and both enthalpic and entropic contributions shape binding, complicating ligand discovery. Here, we analyze three key barriers hindering progress: (1) nontraditional binding mechanisms that challenge classical drug design, (2) experimental and computational limitations for studying disorder, and (3) a lack of systematic datasets. Our analysis of the Biological Magnetic Resonance Data Bank (BMRB) and BindingDB highlights the extreme underrepresentation of IDPs and IDRs, underscoring the need for community-driven data resources. By integrating new binding paradigms, tailored methodologies, and standardized datasets, drug discovery can begin to harness IDPs as a new therapeutic frontier.</div></div>","PeriodicalId":10887,"journal":{"name":"Current opinion in structural biology","volume":"97 ","pages":"Article 103236"},"PeriodicalIF":6.1,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147347623","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
In situ structural studies of membrane protein megacomplexes 膜蛋白巨复合体的原位结构研究
IF 6.1 2区 生物学
Current opinion in structural biology Pub Date : 2026-04-01 Epub Date: 2026-02-12 DOI: 10.1016/j.sbi.2026.103222
Shan Sun, Sen-Fang Sui
{"title":"In situ structural studies of membrane protein megacomplexes","authors":"Shan Sun,&nbsp;Sen-Fang Sui","doi":"10.1016/j.sbi.2026.103222","DOIUrl":"10.1016/j.sbi.2026.103222","url":null,"abstract":"<div><div>Membrane protein complexes are essential for cellular functions, which rely on both constituent protein structures and their interactions within native membranes. While <em>in vitro</em> methods have successfully yielded high-resolution structures of individual proteins and subcomplexes, these approaches typically require detergent extraction and extensive purification, which can disrupt the native membrane environment and potentially alter the supramolecular organization. <em>In situ</em> structural biology has therefore emerged as an effective strategy to overcome these limitations by directly visualizing macromolecular machines within their physiological context. With continuous technological advancements, several recent studies have resolved <em>in situ</em> structures of large protein complexes at high or even near-atomic resolution. This review focuses on recent <em>in situ</em> high-resolution studies of membrane protein megacomplexes, highlighting key technical innovations, structural insights, and the remaining challenges and opportunities in the field.</div></div>","PeriodicalId":10887,"journal":{"name":"Current opinion in structural biology","volume":"97 ","pages":"Article 103222"},"PeriodicalIF":6.1,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146171553","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Rational protein design 合理的蛋白质设计
IF 6.1 2区 生物学
Current opinion in structural biology Pub Date : 2026-04-01 Epub Date: 2026-02-12 DOI: 10.1016/j.sbi.2026.103224
Joel J. Chubb , Aimee L. Boyle , Katherine I. Albanese
{"title":"Rational protein design","authors":"Joel J. Chubb ,&nbsp;Aimee L. Boyle ,&nbsp;Katherine I. Albanese","doi":"10.1016/j.sbi.2026.103224","DOIUrl":"10.1016/j.sbi.2026.103224","url":null,"abstract":"<div><div>Protein design enables the creation of novel structures and functions beyond those found in nature, with recent progress accelerated by computational modeling and machine learning. However, many automated methods act as black boxes, limiting mechanistic insight. Here we highlight the continuing importance of rational protein design, defined as an approach rooted in physical principles, chemical intuition, and sequence–structure–function relationships. We outline three complementary strategies: backbone-first, sequence-first, and function-first, which provide interpretable design frameworks and enable robust scaffold generation, motif incorporation, and functional engineering. Looking forward, we argue that hybrid workflows combining rational principles with machine learning offer the most promising route to dynamic, explainable, and generalizable protein design.</div></div>","PeriodicalId":10887,"journal":{"name":"Current opinion in structural biology","volume":"97 ","pages":"Article 103224"},"PeriodicalIF":6.1,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146171552","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Moving the antibody: Molecular dynamics for molecular mechanisms and developability 移动抗体：分子动力学的分子机制和可展性。
IF 6.1 2区 生物学
Current opinion in structural biology Pub Date : 2026-04-01 Epub Date: 2026-02-18 DOI: 10.1016/j.sbi.2026.103225
Matteo Cagiada , Charlotte M. Deane
{"title":"Moving the antibody: Molecular dynamics for molecular mechanisms and developability","authors":"Matteo Cagiada ,&nbsp;Charlotte M. Deane","doi":"10.1016/j.sbi.2026.103225","DOIUrl":"10.1016/j.sbi.2026.103225","url":null,"abstract":"","PeriodicalId":10887,"journal":{"name":"Current opinion in structural biology","volume":"97 ","pages":"Article 103225"},"PeriodicalIF":6.1,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146225816","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Drug–target residence time: Analyzing cooperativity effects in G protein-coupled receptors by mathematical modeling and molecular dynamics simulations 药物靶停留时间：用数学模型和分子动力学模拟分析G蛋白偶联受体的协同效应。
IF 6.1 2区 生物学
Current opinion in structural biology Pub Date : 2026-04-01 Epub Date: 2026-02-07 DOI: 10.1016/j.sbi.2025.103214
Antonio J. Ortiz , Antoniel A.S. Gomes , Pedro Renault , David Romero , Antoni Guillamon , Jesús Giraldo
{"title":"Drug–target residence time: Analyzing cooperativity effects in G protein-coupled receptors by mathematical modeling and molecular dynamics simulations","authors":"Antonio J. Ortiz ,&nbsp;Antoniel A.S. Gomes ,&nbsp;Pedro Renault ,&nbsp;David Romero ,&nbsp;Antoni Guillamon ,&nbsp;Jesús Giraldo","doi":"10.1016/j.sbi.2025.103214","DOIUrl":"10.1016/j.sbi.2025.103214","url":null,"abstract":"<div><div>Drug–target residence time (τ) is reviewed from two perspectives: mathematics and molecular dynamics. The first focuses on the quantification of τ using a mathematical formalism applicable to different pharmacological mechanistic conditions. This formalism is based on the concept of the smallest-modulus eigenvalue of a subsystem of interest, in which the global formation process has been eliminated. The second includes relevant studies of recent years to provide a structural explanation of τ predictions. Special attention is paid to physically supported artificial intelligence methods. The main objective of this minireview is to promote a combined approach in which mathematics and physics work synergistically to describe the complexity associated with τ in G protein-coupled receptors.</div></div>","PeriodicalId":10887,"journal":{"name":"Current opinion in structural biology","volume":"97 ","pages":"Article 103214"},"PeriodicalIF":6.1,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146141361","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
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