Biomolecular NMR Assignments最新文献_第2页

Backbone resonance assignments of CPEB3 [1–120], CPEB3 [186–315], and CPEB3 [400–459] CPEB3[1-120]、CPEB3[186-315]和CPEB3[400-459]的主干共振分配。

IF 0.6 4区生物学

Biomolecular NMR Assignments Pub Date : 2026-05-29 DOI: 10.1007/s12104-026-10269-2

Yujin Lee, Harunobu Saito, Masatomo So, Ayako Furukawa, Kenji Sugase

引用次数: 0

Backbone resonance assignment of the third domain of the human staphylococcal nuclease domain-containing protein 1 (SND1) 人葡萄球菌核酸酶结构域蛋白1 （SND1）第三结构域的骨干共振分配。

IF 0.6 4区生物学

Biomolecular NMR Assignments Pub Date : 2026-05-16 DOI: 10.1007/s12104-026-10267-4

Shradha Ajith, Liza Cubeddu, Roland Gamsjaeger

{"title":"Backbone resonance assignment of the third domain of the human staphylococcal nuclease domain-containing protein 1 (SND1)","authors":"Shradha Ajith, Liza Cubeddu, Roland Gamsjaeger","doi":"10.1007/s12104-026-10267-4","DOIUrl":"10.1007/s12104-026-10267-4","url":null,"abstract":"<div>Staphylococcal nuclease and Tudor domain‑containing protein 1 (SND1) is a multifunctional RNA‑binding protein implicated in transcriptional regulation, post‑transcriptional RNA control, oncogenesis, and viral infection. Initially identified as a transcriptional coactivator, SND1 was later established as a component of the RNA‑induced silencing complex, where it contributes to RNA turnover and microRNA regulation. SND1’s diverse activities stem from its modular architecture, comprising four staphylococcal nuclease‑like domains, capable of direct RNA binding, and an extended Tudor domain that together form an integrated RNA‑binding and catalytic platform. This versatility also underlies its role in viral infection: SND1 acts as an m⁶A reader and is exploited by RNA viruses, such as SARS‑CoV‑2. Recent work showed that SND1 depletion, particularly loss of its third structured domain (SN3), reduces recruitment of the viral protein Nsp9 to the 3′ untranslated region of the SARS‑CoV‑2 genome, impairing viral RNA synthesis through a direct SN3–Nsp9 interaction. Here, we report expression, purification, and near‑complete backbone NMR assignments of the SN3 domain of SND1. Secondary structure elements calculated by TALOS-N based on these assignments are in good agreement with the existing crystal structure of SN3. Our data provide an excellent foundation for future structural studies of SND1–RNA complexes and their roles in viral RNA priming in SARS-CoV-2.</div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"20 1","pages":""},"PeriodicalIF":0.6,"publicationDate":"2026-05-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13179928/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147959612","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Backbone resonance assignment of the Thalidomide Binding Domain (TBD) of cereblon 小脑沙利度胺结合域（TBD）的骨干共振分配

IF 0.6 4区生物学

Biomolecular NMR Assignments Pub Date : 2026-05-08 DOI: 10.1007/s12104-026-10266-5

Qiwei Huang, Hui Qi Ng, CongBao Kang

引用次数: 0

1H, 13C, 15N backbone assignment of the minimally tied trefoil knot, MTTSA, a 23s rRNA SPOUT methyltransferase 最小三叶结的1H， 13C， 15N骨架分配，MTTSA，一个23s rRNA SPOUT甲基转移酶

IF 0.6 4区生物学

Biomolecular NMR Assignments Pub Date : 2026-04-10 DOI: 10.1007/s12104-026-10262-9

Tiange Tao, Dominique T. Capraro, Patricia A. Jennings

{"title":"1H, 13C, 15N backbone assignment of the minimally tied trefoil knot, MTTSA, a 23s rRNA SPOUT methyltransferase","authors":"Tiange Tao, Dominique T. Capraro, Patricia A. Jennings","doi":"10.1007/s12104-026-10262-9","DOIUrl":"10.1007/s12104-026-10262-9","url":null,"abstract":"<div>\u0000 \u0000 Knotted Methyltransferases (MTase) from the SpoU-TrmD (SPOUT) family offer a unique opportunity to study a protein knot topology and enzymatic function. The knotted methyltransferase from Staphylococcus aureus, MTTSA (PDB: 1vh0, 4fak), is an ɑ/β-knotted 23s rRNA MTase containing only the minimal scaffold among the SPOUT family members. This dimeric enzyme is a minimalist model to study the deep + 31 knot. Here, we report the non-proline backbone assignments with 98.8% completion using TROSY-based NMR experiments on uniformly labeled 2H/13C/15N-labeled protein. Complementary HBHA(CO)NH experiments on 13C/15N-labeled protein were completed for Hα/Hβ sidechain assignments. Both backbone and sidechain assignments were deposited in the Biological Magnetic Resonance Bank (BMRB ID: 53391). Of 164 assigned residues, TALOS-N predictions provided 88.4% unambiguous assignments based on the HN, Hα, Cα, Cβ and N chemical shifts. In addition, the predicted secondary structure based on torsion angles and the ΔδCα-ΔδCβ profile are in agreement with the crystal structures.\u0000 </div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"20 1","pages":""},"PeriodicalIF":0.6,"publicationDate":"2026-04-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s12104-026-10262-9.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147643068","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

1H, 13C and 15N resonance assignments of the N-terminal intrinsically disordered region and WGR domain of human PARP2 人类PARP2基因n端内在无序区和WGR结构域的1H， 13C和15N共振分配。

IF 0.6 4区生物学

Biomolecular NMR Assignments Pub Date : 2026-04-09 DOI: 10.1007/s12104-026-10265-6

Rajbinder K. Virk, Tae Hun Kim

{"title":"1H, 13C and 15N resonance assignments of the N-terminal intrinsically disordered region and WGR domain of human PARP2","authors":"Rajbinder K. Virk, Tae Hun Kim","doi":"10.1007/s12104-026-10265-6","DOIUrl":"10.1007/s12104-026-10265-6","url":null,"abstract":"<div>\u0000 \u0000 Poly(ADP-ribose) polymerase 2 (PARP2) is a key sensor of DNA single-strand breaks that catalyzes ADP-ribosylation of itself and other substrates to initiate DNA repair. Human PARP2 contains an intrinsically disordered N-terminal domain (NTD) that mediates chromatin association and nuclear localization, a central WGR domain that recognizes DNA breaks, and a catalytic domain responsible for poly(ADP-ribose) synthesis. Despite its importance in genome maintenance and as a target of clinical PARP inhibitors, detailed information on the structural and dynamic properties of the NTD and WGR domains has remained limited. Here, we report the 1H, 13C, and 15N resonance assignments of the N-terminal intrinsically disordered region (residues 1–89) and the WGR domain (residues 90–212) of human PARP2. Resonance assignments were first obtained separately for each domain and subsequently transferred to a combined NTD–WGR construct. These assignments provide a foundation for future studies investigating the conformational dynamics, DNA recognition mechanisms, and allosteric regulation of PARP2 in chromatin and repair signaling.\u0000 </div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"20 1","pages":""},"PeriodicalIF":0.6,"publicationDate":"2026-04-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s12104-026-10265-6.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147637583","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Backbone resonance assignment of mucoricin: a step towards structural insights into mucor pathogenesis 毛霉素的骨干共振分配：对毛霉发病机制的结构见解的一步。

IF 0.6 4区生物学

Biomolecular NMR Assignments Pub Date : 2026-04-01 DOI: 10.1007/s12104-026-10264-7

Mansi Tanwar, Priya Yadav, Manish Kumar, Anamika Singh, T. P. Singh, Sujata Sharma, Neel Sarovar Bhavesh, Pradeep Sharma

{"title":"Backbone resonance assignment of mucoricin: a step towards structural insights into mucor pathogenesis","authors":"Mansi Tanwar, Priya Yadav, Manish Kumar, Anamika Singh, T. P. Singh, Sujata Sharma, Neel Sarovar Bhavesh, Pradeep Sharma","doi":"10.1007/s12104-026-10264-7","DOIUrl":"10.1007/s12104-026-10264-7","url":null,"abstract":"<div>\u0000 \u0000 Mucoricin is a key virulence factor in mucormycosis, as it targets host endothelial cells and inhibits protein translation through its N-glycosylase activity, leading to vascular leak and increased vascular permeability, thereby contributing to further disease progression. Its structure is quite unique, being structurally homologous to the Ricin B chain as confirmed by cross-reactivity with monoclonal anti-Ricin B chain antibodies, while exhibiting enzymatic activity similar to the Ricin A chain. Here, we report near-complete backbone (Soliman in Nat Microbiol 6(3):313–326, 2021) 1H, 15N, and 13C chemical shift assignments of Mucoricin from Rhizopus delemar at pH 7.5 using NMR spectroscopy. This represents a critical step toward identifying unique structural elements that contribute to its compact structure and toxin activity, which have remained evolutionarily conserved. The secondary structure probabilities derived from the chemical shift data are well aligned with the predicted AlphaFold model, reinforcing the accuracy of the assigned resonances and the structural integrity of recombinant Mucoricin.\u0000 </div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"20 1","pages":""},"PeriodicalIF":0.6,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147589202","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"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

1H, 13C, and 15N backbone resonance assignments of the A2 domain of human von Willebrand factor 人von Willebrand因子A2结构域的1H， 13C和15N骨干共振分配。

IF 0.6 4区生物学

Biomolecular NMR Assignments Pub Date : 2026-03-23 DOI: 10.1007/s12104-026-10263-8

Ryuichi Hyakumoto, Masatomo So, Ayako Furukawa, Daichi Morimoto, Kenji Sugase

引用次数: 0

Amide 1H and 15N NMR signal assignments of all naturally-occurring di-ubiquitins 所有天然存在的二泛素的酰胺1H和15N核磁共振信号分配。

IF 0.6 4区生物学

Biomolecular NMR Assignments Pub Date : 2026-02-26 DOI: 10.1007/s12104-026-10261-w

Iladeiti Kurbah, Carlos A. Castañeda, David Fushman

{"title":"Amide 1H and 15N NMR signal assignments of all naturally-occurring di-ubiquitins","authors":"Iladeiti Kurbah, Carlos A. Castañeda, David Fushman","doi":"10.1007/s12104-026-10261-w","DOIUrl":"10.1007/s12104-026-10261-w","url":null,"abstract":"<div>Ubiquitin acts as a building block for a wide variety of poly-ubiquitin chains. Decoding the role of poly-ubiquitin chains in different cellular processes remains an active area of research. Here, we report amide 1H and 15N signal assignments of each ubiquitin unit in di-ubiquitins of all seven lysine linkages and in M1-linked di-ubiquitin determined by our lab over the last decade. These assignments can aid in NMR studies of the structure, dynamics, and function of various di-ubiquitins. Comparison of the NMR resonance assignments among all the di-ubiquitins revealed linkage-specific chemical shifts and isopeptide signals that can be used as “fingerprints” to directly identify using NMR spectroscopy the linkage type in a di-ubiquitin and potentially longer poly-ubiquitin chains. Our data highlight both the similarities and dissimilarities of NMR signals of ubiquitin units in di-ubiquitins of different linkages, as well as the importance of selective isotopic labeling of specific ubiquitin units in a poly-ubiquitin chain for NMR studies.</div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"20 1","pages":""},"PeriodicalIF":0.6,"publicationDate":"2026-02-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12935793/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147300695","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

1H, 13C and 15N resonance assignments for human all-Ala α-lactalbumin in its molten globule and urea-denatured states 人全α α-乳清蛋白在熔融球态和尿素变性态的1H、13C和15N共振分配

IF 0.6 4区生物学

Biomolecular NMR Assignments Pub Date : 2026-01-23 DOI: 10.1007/s12104-026-10260-x

Lorena Varela, Lorna J. Smith, Christina Redfield

{"title":"1H, 13C and 15N resonance assignments for human all-Ala α-lactalbumin in its molten globule and urea-denatured states","authors":"Lorena Varela, Lorna J. Smith, Christina Redfield","doi":"10.1007/s12104-026-10260-x","DOIUrl":"10.1007/s12104-026-10260-x","url":null,"abstract":"<div>Molten globules are compact, partially-folded proteins postulated to be general intermediates in protein folding. Human α-lactalbumin (α-LA) is a Ca2+-binding, four-disulphide protein whose native structure is divided into two lobes, one is largely helical, the α-domain, and the other has a significant β-sheet content, the β-domain. α-LA forms a “classical” molten globule at low pH which has been studied widely as a model system of a partially-folded protein. The α-LA molten globule is compact and has a native-like helical secondary structure content. All-Ala α-LA, which has all eight native cysteines mutated to alanine, also adopts a partially-folded molten globule conformation and gives a high-quality 1H-15N HSQC spectrum at pH 2 and 40 °C. The lack of cysteine residues makes all-Ala α-LA a suitable template for spin-labelling studies. In this report we present 1H, 13C and 15N assignments for human all-Ala α-LA in its molten globule and 8 M urea-denatured states. Analysis of the chemical shift data for the molten globule state shows they are consistent with high populations of conformations in the α region of φ,ψ space for residues in the α domain of the protein. In contrast, the data for the urea-denatured state are closely similar to those expected for a random coil.</div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"20 1","pages":""},"PeriodicalIF":0.6,"publicationDate":"2026-01-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s12104-026-10260-x.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146027451","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Backbone resonance assignment of the pentraxin domain of the neuronal pentraxin receptor (NPTXR) 神经元戊烷素受体（NPTXR）戊烷素结构域的骨干共振分配。

IF 0.6 4区生物学

Biomolecular NMR Assignments Pub Date : 2026-01-07 DOI: 10.1007/s12104-025-10259-w

Alexandra K. Pozhidaeva, Yunfeng Li, Yulia Pustovalova, Jeffrey C. Hoch, David C. Martinelli, Bernd Simon, Bing Hao

引用次数: 0