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TMEM55B-Jack of all trades in the endo-lysosomal system? tmem55b -内溶酶体系统中最杰出的？

IF 4.3 2区生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY

Structure

Pub Date : 2026-02-05 DOI: 10.1016/j.str.2025.12.012

Markus Damme, Daniel Kümmel

In this issue of Structure, Waschbüsch et al.¹ report structural and proteomics studies of TMEM55B, a transmembrane protein implicated in a variety of lysosomal functions. The authors identify a binding motif in several client proteins that interact with TMEM55B. This study provides key insights for future investigations of TMEM55B's molecular functions.

在本期《结构》杂志上，waschb等人报道了TMEM55B的结构和蛋白质组学研究，TMEM55B是一种涉及多种溶酶体功能的跨膜蛋白。作者在几个与TMEM55B相互作用的客户蛋白中发现了一个结合基序。这项研究为未来研究TMEM55B的分子功能提供了关键的见解。

引用次数: 0

Meet the authors: Cong-Zhao Zhou and Yong-Liang Jiang. 认识一下作者：周聪昭和蒋永亮。

IF 4.3 2区生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY

Structure

Pub Date : 2026-02-05 DOI: 10.1016/j.str.2026.01.004

Cong-Zhao Zhou, Yong-Liang Jiang

In this meet-the-authors Q&A, Structure Editor-in-Chief Karin Kühnel speaks to Cong-Zhao Zhou and Yong-Liang Jiang from the University of Science and Technology of China in Hefei about their recent Structure paper entitled "Cryo-EM structure of cyanopodophage Pan3 reveals a modular tail architecture for host recognition" and their research and careers.

在本次作者见面会中，Structure主编Karin k hnel采访了中国科学技术大学的周从招和蒋永亮，介绍了他们最近发表的题为《cyanopodophage Pan3的Cryo-EM结构揭示了宿主识别的模块化尾部结构》的Structure论文，以及他们的研究和职业生涯。

引用次数: 0

NMR, a tool for biology. 核磁共振，一个生物学的工具。

IF 4.3 2区生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY

Structure

Pub Date : 2026-02-05 DOI: 10.1016/j.str.2025.12.013

Nadia Izadi-Pruneyre, Michael Nilges

Every 2 years the "NMR, a tool for biology" conference brings together renowned experts and emerging scientists to explore the application of nuclear magnetic resonance (NMR) in addressing fundamental biological questions. This international event in Paris showcases the latest methodological and application advances that reinforce NMR's impact in structural biology. Here, we present key highlights from the XIVth edition.

每两年一次的“核磁共振，生物学的工具”会议汇集了知名专家和新兴科学家，探讨核磁共振（NMR）在解决基本生物学问题中的应用。这次在巴黎举行的国际活动展示了最新的方法和应用进展，加强了核磁共振在结构生物学中的影响。在这里，我们介绍第十四版的主要亮点。

引用次数: 0

Structural basis for pan-coronavirus inhibition of 3CL protease. 泛冠状病毒抑制3CL蛋白酶的结构基础。

IF 4.3 2区生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY

Structure

Pub Date : 2026-02-05 DOI: 10.1016/j.str.2026.01.003

Eswar R Reddem, Farhad Forouhar, Cheng Liu, Sarah K Stevens, Andreas Jekle, Ching-Wen Chang, Neelam Oswal, David C McGowan, Koen Vandyck, David B Smith, Pierre Raboisson, Leonid N Beigelman, Phinikoula S Katsamba, Fabiana Bahna, Seetha Mannepalli, Lawrence Blatt, David Perlin, Julian A Symons, Lawrence Shapiro, Antitsa D Stoycheva

Epidemic and pandemic outbreaks of respiratory illness caused by three different coronaviruses over the past two decades have underscored the importance of pharmaceutical agents that could offer broad-spectrum activity across this family of pathogens. Two coronavirus inhibitors characterized by broad in vitro potency were synthesized and studied with X-ray crystallography. Their high-resolution structures in complex with six α-, β-, and γ-coronaviruses delineate the requirements for pan-coronavirus inhibition by drug-like molecules targeting the S1-S4 subsites of the viral 3CL-protease, which performs a critical function during coronavirus polyprotein processing. Anchoring by polar contacts in S1, utilization of hydrophobic packing in S2, compact substitutions in S3, and mid-sized hydrophobic modifications in S4 are all factors contributing to inhibitor activity. Interactions in S2 are modulated by the amino acid identity of three key residues, and in S4, where sequence conservation is the lowest, pan-coronavirus coverage is facilitated by solvent exposure of the diverging side chains.

在过去二十年中，由三种不同的冠状病毒引起的呼吸系统疾病的流行和大流行爆发，突显了能够在这一病原体家族中提供广谱活性的药物的重要性。合成了两种具有广泛体外效价的冠状病毒抑制剂，并用x射线晶体学对其进行了研究。它们与6种α-、β-和γ-冠状病毒复合物的高分辨率结构描述了靶向病毒3cl蛋白酶S1-S4亚位的药物样分子对泛冠状病毒的抑制需求，3cl蛋白酶在冠状病毒多蛋白加工过程中起关键作用。S1中的极性接触锚定、S2中疏水填料的利用、S3中的致密取代以及S4中疏水修饰都是影响抑制剂活性的因素。S2中的相互作用由三个关键残基的氨基酸特性调节，而在序列保守性最低的S4中，发散侧链的溶剂暴露有助于泛冠状病毒的覆盖。

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引用次数: 0

Defining the mechanism of cross-reactivity for a SARS-CoV-2 Beta-elicited antibody toward omicron sub-lineages 确定SARS-CoV-2 β诱导抗体对组粒亚谱系的交叉反应性机制

IF 5.7 2区生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY

Structure

Pub Date : 2026-02-04 DOI: 10.1016/j.str.2026.01.006

Frances Ayres, Bronwen Lambson, Nonhlanhla N. Mkhize, Zanele Makhado, Donald Mhlanga, Rudolph Serage, Penny L. Moore, Constantinos Kurt Wibmer, Thandeka Moyo-Gwete

Despite the continual emergence of SARS-CoV-2 variants and increasing diversity within the receptor binding domain (RBD), some antibody responses that are directed to conserved regions can display cross-reactivity against variants. We previously isolated an RBD-directed monoclonal antibody (084-7D) from a Beta-infected donor that neutralized Beta and emerging Omicron variants. Here, we solved a high-resolution crystal structure of the 084-7D Fab in complex with the Beta RBD. These data revealed an epitope overlapping both the ACE2 binding site and those of other class 1 antibodies. Furthermore, the epitope includes highly conserved residues, Q409, D420, and Y489, that are present in recent Omicron variants. The N417 residue that emerged with Beta and has since persisted is tolerated within the epitope of 084-7D, explaining the preferential neutralization of contemporaneous N417-containing variants. These structural data defined the mechanism for cross-reactivity of a Beta-elicited neutralizing antibody, potentially informing the design of future broadly reactive SARS-CoV-2 therapeutics.

尽管SARS-CoV-2变体不断出现，并且受体结合域（RBD）内的多样性不断增加，但一些针对保守区域的抗体反应可以对变体表现出交叉反应性。我们之前从β感染的供体中分离出一种rbd定向单克隆抗体（084-7D），该抗体可以中和β和新出现的Omicron变体。在这里，我们用Beta RBD解决了084-7D Fab复合物的高分辨率晶体结构。这些数据揭示了ACE2结合位点和其他1类抗体的表位重叠。此外，表位包括高度保守的残基Q409、D420和Y489，这些残基存在于最近的Omicron变体中。与β一起出现并持续存在的N417残基在084-7D的表位内是耐受的，这解释了同时含有N417的变异的优先中和。这些结构数据定义了β诱导的中和抗体交叉反应性的机制，可能为未来广泛反应性SARS-CoV-2疗法的设计提供信息。

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引用次数: 0

Structural repertoire of HCV broadly neutralizing antibodies targeting the E2 front layer supersite 针对E2前层超位点的HCV广泛中和抗体的结构库

IF 5.7 2区生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY

Structure

Pub Date : 2026-02-02 DOI: 10.1016/j.str.2026.01.005

Xander E. Wilcox, Rajat Punia, Jessica Mimms, Nicole Frumento, Justin R. Bailey, Andrew I. Flyak

引用次数: 0

Discovery of tankyrase scaffolding inhibitor specifically targeting the ARC4 peptide binding domain 特异性靶向ARC4肽结合域的坦克酶脚手架抑制剂的发现

IF 5.7 2区生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY

Structure

Pub Date : 2026-01-30 DOI: 10.1016/j.str.2025.12.015

Chiara Bosetti, Albert Galera-Prat, Sven T. Sowa, Alexandra Gade, Cláudia Braga, Shoshy A. Brinch, Faranak Nami, Johan Pääkkönen, Veeti Pulju, Maureen T. Meling, Maria Candamo-Lourido, Jo Waaler, Mads H. Clausen, Lari Lehtiö

Tankyrases are poly-ADP-ribosyltransferases that orchestrate numerous biological processes involved in disease. Their established regulatory roles, particularly within the WNT/β-catenin pathway, have driven notable drug discovery efforts aimed at inhibiting their catalytic activity. Targeting tankyrases’ interaction with proteins through their ARC domains represents an alternative strategy to be explored as a therapeutic approach against specific protein-protein interactions. In this article, we employed a pre-established FRET-based assay to screen the EU-OPENSCREEN libraries for identification of ARC4 inhibitors. We discovered a series of pyrrolone-based compounds, and we synthesized compound S8 (ARCher-142), which binds selectively to ARC4 with a potency of 8 μM. NMR analysis and X-ray crystallography allowed us to identify the binding site and to rationalize the observed selectivity. Despite binding exclusively to ARC4, the inhibitor can attenuate the WNT/β-catenin signaling pathway in cells. Our work demonstrates that targeting single ARC domains is possible, offering an inhibition approach tailored to tankyrase ARC4.

tankyase是一种多聚adp -核糖基转移酶，它协调了许多与疾病有关的生物过程。它们已确立的调节作用，特别是在WNT/β-catenin通路中，已推动了旨在抑制其催化活性的显著药物发现工作。靶向坦克酶通过其ARC结构域与蛋白质的相互作用代表了一种替代策略，作为一种针对特定蛋白质相互作用的治疗方法。在本文中，我们采用预先建立的基于fret的检测方法筛选EU-OPENSCREEN文库以鉴定ARC4抑制剂。我们发现了一系列吡咯酮类化合物，并合成了化合物S8 (ARCher-142)，该化合物与ARC4选择性结合，效价为8 μM。核磁共振分析和x射线晶体学使我们能够确定结合位点并使观察到的选择性合理化。尽管只与ARC4结合，但该抑制剂可以减弱细胞中的WNT/β-catenin信号通路。我们的工作表明，靶向单个ARC结构域是可能的，提供了一种针对坦克酶ARC4的抑制方法。

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引用次数: 0

A mechanistic understanding of how KCNE1 tunes KCNQ1 channel pharmacology KCNE1如何调节KCNQ1通道药理学的机制理解

IF 5.7 2区生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY

Structure

Pub Date : 2026-01-29 DOI: 10.1016/j.str.2026.01.002

Yahnell Judah, Jessica J. Jowais, Valentina Corradi, Marta E. Perez, Rene Barro-Soria, D. Peter Tieleman, H. Peter Larsson

引用次数: 0

Time-resolved X-ray solution scattering observations of light-induced structural changes in sensory rhodopsin II 光致感觉视紫红质结构变化的时间分辨x射线溶液散射观察

IF 5.7 2区生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY

Structure

Pub Date : 2026-01-26 DOI: 10.1016/j.str.2025.12.014

Lucija Ostojić, Daniel Sarabi, Robert Bosman, Giorgia Ortolani, Swagatha Ghosh, Martin Nors Pedersen, Mathias Sander, Petra Båth, Greger Hammarin, Robert Dods, Per Norder, Cecilia Safari, Michael Wulff, Matteo Levantino, Gisela Brändén, Richard Neutze

Unicellular organisms respond to a changing environment through physical and chemical sensory cascades. Sensory rhodopsin II (SRII) is a blue-light receptor, which initiates a negative phototaxis response in the host archaea. Here, we apply time-resolved X-ray solution scattering (TR-XSS) to characterize the mechanism of signal transduction by SRII and explore how light-induced structural changes are modified when SRII is in complex with its transducer protein (HtrII). TR-XSS difference data are modeled as arising from an outward movement of helices E and F in combination with modest changes associated with helices C and the extracellular regions of helices D and E. The magnitude of the displacement of helices E and F is similar irrespective of whether or not HtrII is present. In combination with structural predictions of the full SRII:HtrII complex, TR-XSS provides insight into how conformational changes may be communicated from SRII to the signaling domain of HtrII.

单细胞生物通过物理和化学感觉级联反应不断变化的环境。感觉视紫红质II （SRII）是一种蓝光受体，在宿主古细菌中引发负的趋光反应。本文采用时间分辨x射线溶液散射（TR-XSS）技术表征SRII的信号转导机制，并探讨SRII与其换能器蛋白（HtrII）复合时，光诱导的结构变化是如何被修饰的。TR-XSS差异数据被建模为由螺旋E和F的向外移动以及与螺旋C和螺旋D和E的细胞外区域相关的适度变化引起的。无论是否存在HtrII，螺旋E和F的位移幅度都是相似的。结合对整个SRII:HtrII复合体的结构预测，TR-XSS提供了关于构象变化如何从SRII传递到HtrII信号域的见解。

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引用次数: 0

Alphafold 3-guided insights into the Importinβ: Importin7 heterodimer interaction and its binding to histone H1 Alphafold 3引导的Importinβ: Importin7异源二聚体相互作用及其与组蛋白H1结合的见解

IF 5.7 2区生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY

Structure

Pub Date : 2026-01-12 DOI: 10.1016/j.str.2025.12.011

Piotr Neumann, Olexandr Dybkov, Henning Urlaub, Ralf Ficner, Achim Dickmanns

The nuclear import of H1 linker histones is facilitated by a heterodimer of the transport receptors Importinβ (Impβ) and Importin7 (Imp7). The interaction between them is mediated by a stretch of C-terminal residues of Imp7 essential also for Imp7 activation by Impβ. An Impβ:Imp7:H1 complex model was predicted by Alphafold3 and validated using cross-linking data, isothermal titration calorimetry, and pull-down experiments, providing robust support for its accuracy. This model positions the H1 globular domain within the central cavity of Imp7. Refinement of this atomic model against a published cryo-electron microscopy (cryo-EM) map demonstrated significantly improved correspondence compared to the earlier interpretation, which placed the H1 globular domain within Impβ. This enhanced structural consistency further substantiates the accuracy of the AI-driven prediction. Moreover, a detailed analysis confirmed the extended C-terminal stretch of Imp7 harboring a nucleoporin-like binding (NlB) region with two FXFG-like nucleoporin motifs interacting with the outer surface of Impβ.

转运受体Importinβ (Impβ)和Importin7 （Imp7）的异源二聚体促进了H1连接体组蛋白的核输入。它们之间的相互作用是由Imp7的一段c端残基介导的，这也是Imp7被Impβ激活所必需的。利用Alphafold3预测了Impβ:Imp7:H1复合物模型，并通过交联数据、等温滴定量热法和下拉实验对其进行了验证，为其准确性提供了强有力的支持。该模型将H1球形结构域定位在Imp7的中心空腔内。根据已发表的冷冻电子显微镜（cryo-EM）图对该原子模型进行了改进，与早期的解释相比，该解释显着改善了相关性，后者将H1球形结构域置于Impβ中。这种增强的结构一致性进一步证实了人工智能驱动的预测的准确性。此外，详细的分析证实，Imp7的c端延伸包含一个核孔蛋白样结合（NlB）区域，两个fxfg样核孔蛋白基序与Impβ的外表面相互作用。

引用次数: 0

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