Biomolecular NMR Assignments最新文献

Backbone and side‑chain 1H, 13C, and 15N resonance assignments and secondary structure determination of human UCHL3 人UCHL3的主链和侧链1H、13C和15N共振赋值和二级结构测定。

IF 0.5 4区生物学

Biomolecular NMR Assignments Pub Date : 2026-11-04 DOI: 10.1007/s12104-026-10287-0

Shigeharu Kubota, Hikari Sato, Hiroki Miyata, Haruka Sugasawa, Yutaka Ito, Teppei Ikeya

{"title":"Backbone and side‑chain 1H, 13C, and 15N resonance assignments and secondary structure determination of human UCHL3","authors":"Shigeharu Kubota, Hikari Sato, Hiroki Miyata, Haruka Sugasawa, Yutaka Ito, Teppei Ikeya","doi":"10.1007/s12104-026-10287-0","DOIUrl":"10.1007/s12104-026-10287-0","url":null,"abstract":"<div>Ubiquitin carboxyl-terminal hydrolase isozyme L3 (UCHL3) is a member of the ubiquitin C-terminal hydrolase (UCH) subfamily of deubiquitinating enzymes (DUBs) which regulate the ubiquitin-proteasome system by cleaving ubiquitin moieties from target proteins or ubiquitin precursors. UCHL3 exhibits diverse physiological functions including cell cycle regulation, the DNA damage response, and chromosome biorientation and segregation. Abnormal UCHL3 activity has been associated with the pathogenesis of various diseases, including breast, lung, and pancreatic cancers, yet the detailed molecular mechanisms underlying these functions remain poorly understood. Previous studies have suggested that the active sites of UCHL3 and other homologous UCHs exhibit substantial dynamics particularly in their enzymatic active site, which may be essential for ubiquitin recognition and enzymatic activity. To provide a structural basis for elucidating the dynamic behavior and functional mechanism of human UCHL3, here we report extensive NMR backbone and side-chain 1H, 13C, and 15N resonance assignments of the recombinant full-length human UCHL3 in solution.</div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"20 1","pages":""},"PeriodicalIF":0.5,"publicationDate":"2026-11-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149331974","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

Backbone and side-chain NMR resonance assignments of Ciona intestinalis(beta gamma)-crystallin 鸡肠草主链和侧链核磁共振配位[公式：见原文]-结晶蛋白。

IF 0.5 4区生物学

Biomolecular NMR Assignments Pub Date : 2026-11-01 DOI: 10.1007/s12104-026-10280-7

Matthew D. Jimenez, Mina Mozafari, Cat Tuong Nguyen Hoang, Miram Ali Al-Botaif, Jeongwoo Ko, Rachel W. Martin

{"title":"Backbone and side-chain NMR resonance assignments of Ciona intestinalis(beta gamma)-crystallin","authors":"Matthew D. Jimenez, Mina Mozafari, Cat Tuong Nguyen Hoang, Miram Ali Al-Botaif, Jeongwoo Ko, Rachel W. Martin","doi":"10.1007/s12104-026-10280-7","DOIUrl":"10.1007/s12104-026-10280-7","url":null,"abstract":"<div>The structural (beta gamma)-crystallin from the tunicate Ciona intestinalis serves as an evolutionary waypoint between ancestral metal cation-binding crystallins and the (beta gamma) crystallins of the vertebrate eye lens. Ci-(beta gamma) maintains the metal cation-binding sites of ancestral crystallins while also sharing common structural motifs with vertebrate lens crystallins. Due to its structure and strong interaction with Ca(^{2+}), Ci-(beta gamma) is more thermally and chemically stable than vertebrate lens crystallins, making it an ideal starting point for understanding (beta gamma) crystallins’ evolution for molecular stability. In this study, we present the side-chain and updated backbone resonance assignments of Ci-(beta gamma) with TALOS-N predictions on the H(_N), H(_alpha), C(_alpha), C(_beta) and N chemical shifts. These assignments provide a foundation for future studies of metal binding, dynamics, and stability of proteins in the (beta gamma)-crystallin family.</div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"20 1","pages":""},"PeriodicalIF":0.5,"publicationDate":"2026-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13724631/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149316939","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 backbone resonance assignment of the N-terminal 280 amino acids of human NHERF1 protein 人NHERF1蛋白n端280个氨基酸的1H， 13C和15N主链共振分配。

IF 0.5 4区生物学

Biomolecular NMR Assignments Pub Date : 2026-10-29 DOI: 10.1007/s12104-026-10281-6

Almudena Hornero-Romera, Miguel Á. Treviño, David Pantoja-Uceda, Jaime Millán, M. Ángeles Jiménez

{"title":"1H, 13C, and 15N backbone resonance assignment of the N-terminal 280 amino acids of human NHERF1 protein","authors":"Almudena Hornero-Romera, Miguel Á. Treviño, David Pantoja-Uceda, Jaime Millán, M. Ángeles Jiménez","doi":"10.1007/s12104-026-10281-6","DOIUrl":"10.1007/s12104-026-10281-6","url":null,"abstract":"<div>NHERF1 (Na+/H+ exchanger regulatory factor-1) is a membrane-associated scaffold protein that links membrane receptors and channels to the actin cytoskeleton. It plays key roles in protein trafficking, signaling, and liver physiology. NHERF1 is a 358-residue long multidomain protein consisting of two PDZ domains, followed by a largely disordered region and a C-terminal ezrin-binding (EB) domain. In the liver, NHERF1 promotes the assembly of complexes containing ERM (ezrin-radixin-moesin) proteins, ICAM-1 (type I transmembrane protein intercellular adhesion molecule), and F-actin. Recent pull-down experiments have suggested that both PDZ1 and PDZ2 domains contribute to ICAM-1 binding. Characterization of this interaction by NMR chemical shift mapping requires a construct containing both PDZ domains. Although NMR studies have previously been reported for the individual PDZ1 and PDZ2 domains, as well as for the full-length NHERF1, no assignments were available for a construct containing only the PDZ domains. Full-length NHERF1 is not adequate for investigating PDZ-mediated interactions because its C-terminal EB domain interacts with PDZ2, causing resonance line broadening. In addition, the full-length 358-residue protein is expected to exhibit greater spectral overlap than a shorter construct. Here, we report the 1H, 15N, and 13C backbone resonance assignments of a N-terminal 280 residue long NHERF1 construct encompassing both the PDZ1 and PDZ2 domains, thereby facilitating future studies of its interactions with ICAM-1 and other binding partners.</div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"20 1","pages":""},"PeriodicalIF":0.5,"publicationDate":"2026-10-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13719848/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149293838","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

Chemical shift assignments of the dimerization domain of NF-KappaB c-Rel subunit NF-KappaB c-Rel亚基二聚化结构域的化学位移赋值。

IF 0.5 4区生物学

Biomolecular NMR Assignments Pub Date : 2026-10-25 DOI: 10.1007/s12104-026-10282-5

Sayan Pal, Mrunal Nanda, Sulakshana P. Mukherjee

引用次数: 0

1H, 13C, and 15N resonance assignments and solution structure of the first double-stranded RNA-binding domain of DExH-Box Helicase 30 (DHX30) DExH-Box解旋酶30 （DHX30）第一双链rna结合域的1H、13C和15N共振分配和溶液结构

IF 0.5 4区生物学

Biomolecular NMR Assignments Pub Date : 2026-10-09 DOI: 10.1007/s12104-026-10279-0

Chikage Abe, Yutaka Muto, Fahu He, Mari Takahashi, Kengo Tsuda, Takashi Nagata, Akiko Tanaka, Naohiro Kobayashi, Takanori Kigawa, Peter Güntert, Mikako Shirouzu, Shigeyuki Yokoyama, Kanako Kuwasako

{"title":"1H, 13C, and 15N resonance assignments and solution structure of the first double-stranded RNA-binding domain of DExH-Box Helicase 30 (DHX30)","authors":"Chikage Abe, Yutaka Muto, Fahu He, Mari Takahashi, Kengo Tsuda, Takashi Nagata, Akiko Tanaka, Naohiro Kobayashi, Takanori Kigawa, Peter Güntert, Mikako Shirouzu, Shigeyuki Yokoyama, Kanako Kuwasako","doi":"10.1007/s12104-026-10279-0","DOIUrl":"10.1007/s12104-026-10279-0","url":null,"abstract":"<div>DHX30 is a member of the DExH-box helicase family and contains two double-stranded RNA-binding domains (dsRBDs) N-terminal to the helicase core domain. DHX30 plays a fundamental role in regulating the translation of transcripts encoding mitoribosomal proteins, thereby facilitating mitoribosome biogenesis. Additionally, DHX30 is involved in the formation of stress granules. These intracellular structures are composed of proteins and RNAs, including mRNAs, and form under stress conditions in association with translational repression. Recent studies have demonstrated that pathogenic mutations in DHX30 underlie a severe neurodevelopmental disorder termed neurodevelopmental disorder with variable motor and language impairment (NEDMIAL), possibly in part through aberrant stress-granule formation. Structural characterization of these RNA-binding domains is an important step toward understanding the molecular basis of DHX30 function. In this study, we focus on the first dsRBD (dsRBD-1) of human DHX30 and report its 1H, 13C, and 15N resonance assignments and solution structure. DHX30 dsRBD-1 adopts an α0–α1–α1′–β1–β2–β3–α2–α3 topology, with three additional helices (α0, α1′, and α3) relative to the canonical dsRBD topology (α1–β1–β2–β3–α2). To our knowledge, this is the first experimentally determined structure of a DHX30 domain. These resonance assignments and structural insights provide a valuable foundation for future structural and functional studies of DHX30.</div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"20 1","pages":""},"PeriodicalIF":0.5,"publicationDate":"2026-10-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149132795","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

Backbone and side chain 1H, 13C and 15N chemical shift assignment of the cargo-recognition domain MOTH of human TANGO1 人类tango - 1的主侧链1H， 13C和15N的化学位移分配

IF 0.5 4区生物学

Biomolecular NMR Assignments Pub Date : 2026-09-11 DOI: 10.1007/s12104-026-10278-1

Jelena Auch, Anna Carlotta Peddinghaus, Raphael Stoll

{"title":"Backbone and side chain 1H, 13C and 15N chemical shift assignment of the cargo-recognition domain MOTH of human TANGO1","authors":"Jelena Auch, Anna Carlotta Peddinghaus, Raphael Stoll","doi":"10.1007/s12104-026-10278-1","DOIUrl":"10.1007/s12104-026-10278-1","url":null,"abstract":"<div>The cellular export of large-sized proteins, such as collagen or fibrillin, necessitates a specialized transport pathway tailored towards their size. For collagen and possibly also other bulky proteins, the Transport ANd Golgi Organization 1 (TANGO1) protein plays a substantial role in the transfer from the Endoplasmic Reticulum (ER) to the Golgi apparatus. TANGO1 and related proteins organize the ER exit sites and generate large export structures within the cytosol while anchored to the ER membrane. In contrast to other proteins involved, TANGO1 features a folded domain in the ER lumen, which seems to be central for detecting cargos. This cargo-recognition domain has been shown to bind the collagen-specific chaperone HSP47 (Ishikawa et al. 2016) as well as type IV collagen directly (Arnolds and Stoll 2023). However, the exact molecular mechanism of these interactions remains unknown. The resonance assignments presented here lay the foundation for the experiments studying the binding process on a molecular level and is designed to facilitate investigations into how TANGO1 detects and selects the cargos to be exported.</div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"20 1","pages":""},"PeriodicalIF":0.5,"publicationDate":"2026-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s12104-026-10278-1.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148927861","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

The 1H, 15N and 13C backbone resonance assignments of an intrinsically disordered region (467–696) of breast cancer type 1 susceptibility protein (BRCA1) 乳腺癌1型易感蛋白（BRCA1）内在无序区（467-696）的1H， 15N和13C骨干共振分配

IF 0.5 4区生物学

Biomolecular NMR Assignments Pub Date : 2026-09-04 DOI: 10.1007/s12104-026-10277-2

Hoang H. Dinh, Angela M. Jasper, Antoine Baudin, Patrick Sung, David S. Libich

{"title":"The 1H, 15N and 13C backbone resonance assignments of an intrinsically disordered region (467–696) of breast cancer type 1 susceptibility protein (BRCA1)","authors":"Hoang H. Dinh, Angela M. Jasper, Antoine Baudin, Patrick Sung, David S. Libich","doi":"10.1007/s12104-026-10277-2","DOIUrl":"10.1007/s12104-026-10277-2","url":null,"abstract":"<div>The tumor suppressor protein breast cancer type 1 susceptibility protein (BRCA1) plays a central role in maintaining genome stability through its involvement in DNA damage repair, transcriptional regulation, and cell-cycle control. BRCA1 functions as an obligate heterodimer with its binding partner, the BRCA1-associated RING domain protein 1 (BARD1), to coordinate accurate DNA repair. While the structured N- and C-terminal domains of BRCA1 have been well-characterized, the large central region encoded largely by exon 11 that comprises ~ 80% of the protein, is intrinsically disordered, and remains poorly structurally characterized. This intrinsically disordered region (IDR) harbors critical interaction interfaces for key proteins involved in genome maintenance, including RAD50, RAD51, MYC, and RB. Here, we report the backbone resonance assignments of a BRCA1 IDR construct spanning residues 467–696, providing a foundation for future studies aimed at understanding how the disordered central region of BRCA1 contributes to homologous recombination, interactions with BARD1, and overall BRCA1 tumor suppressor function.</div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"20 1","pages":""},"PeriodicalIF":0.5,"publicationDate":"2026-09-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13541922/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148885922","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

The1H, 15N and13C backbone resonance assignments of an intrinsically disordered region (124–270) of BRCA1 associated RING domain 1 (BARD1) BRCA1相关环结构域1 （BARD1）的内在无序区（124-270）的1h， 15N和13c骨干共振分配。

IF 0.5 4区生物学

Biomolecular NMR Assignments Pub Date : 2026-09-01 DOI: 10.1007/s12104-026-10276-3

Hoang H. Dinh, Angela M. Jasper, Antoine Baudin, Patrick Sung, David S. Libich

{"title":"The1H, 15N and13C backbone resonance assignments of an intrinsically disordered region (124–270) of BRCA1 associated RING domain 1 (BARD1)","authors":"Hoang H. Dinh, Angela M. Jasper, Antoine Baudin, Patrick Sung, David S. Libich","doi":"10.1007/s12104-026-10276-3","DOIUrl":"10.1007/s12104-026-10276-3","url":null,"abstract":"<div>The BRCA1-associated RING domain protein 1 (BARD1) is the obligate binding partner of the tumor suppressor breast cancer type 1 susceptibility protein (BRCA1) and plays a critical role in maintaining genome integrity. BARD1 contains structured N- and C-terminal domains that mediate heterodimerization with BRCA1, recognition of chromatin marks, and DNA repair functions. Approximately 40% of BARD1 is intrinsically disordered, particularly in the central region of the protein. This intrinsically disordered region (IDR) engages DNA and key repair proteins such as RAD51, BLM, and WRN. DNA binding through the BARD1 IDR facilitates H2A ubiquitination by the BRCA1-BARD1 complex and is essential for stimulating long-range DNA end resection during homologous recombination, underscoring its role in accurate DNA repair. Despite these insights, structural characterization of the IDR remains limited, leaving questions regarding its functional interplay with BRCA1 and other repair factors unresolved. Here, we report the backbone resonance assignments of a BARD1 IDR construct spanning residues 124–270, providing a foundation for future studies aimed at understanding how the disordered regions of BARD1 interact with various binding partners, and cooperates with itself and BRCA1 to regulate genome stability.</div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"20 1","pages":""},"PeriodicalIF":0.5,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13534175/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148872437","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 backbone and side-chain resonance assignments of the Nostoc sp. H-NOX C139A variant in complex with the soluble Guanylyl Cyclase inhibitor Zinc Protoporphyrin IX Nostoc sp. H-NOX C139A突变体与可溶性环化酶抑制剂锌原卟啉IX配合物的1H， 13C和15N主链和侧链共振分配。

IF 0.5 4区生物学

Biomolecular NMR Assignments Pub Date : 2026-08-26 DOI: 10.1007/s12104-026-10274-5

Stefanos I. Gravalos, Emmanouil N. Andreadis, Francesca Cantini, Lucia Banci, Georgios A. Spyroulias

{"title":"1H, 13C, and 15N backbone and side-chain resonance assignments of the Nostoc sp. H-NOX C139A variant in complex with the soluble Guanylyl Cyclase inhibitor Zinc Protoporphyrin IX","authors":"Stefanos I. Gravalos, Emmanouil N. Andreadis, Francesca Cantini, Lucia Banci, Georgios A. Spyroulias","doi":"10.1007/s12104-026-10274-5","DOIUrl":"10.1007/s12104-026-10274-5","url":null,"abstract":"<div>The H-NOX (Heme–Nitric oxide/Oxygen binding) domain is highly conserved among both eukaryotes and bacteria. In human soluble Guanylyl Cyclase (sGC), the H-NOX domain functions as a sensor for the gaseous signaling molecule Nitric Oxide (NO). Located at the N-terminus of the enzyme, the heme B-binding H-NOX domain regulates the catalytic domain at the C-terminus, which catalyzes the conversion of GTP (guanosine 5′-triphosphate) to cGMP (cyclic Guanosine MonoPhosphate). The present study employs the bacterial homolog Nostoc sp. H-NOX (Ns H-NOX) C139A mutant together with the sGC inhibitor Zinc Protoporphyrin IX (ZnPPIX) as experimental tools to investigate the still poorly understood mechanisms underlying sGC activation and inhibition, and to elucidate either the chemical features of novel scaffolds associated with a new class of activators, or the distinct activities imposed by two prosthetic groups sharing the same organic framework, but differing in the chelated transition metal. Here, we present the conditions employed for the formation of the complex between the Ns H-NOX C139A mutant and the sGC inhibitor ZnPPIX, together with the UV–Vis absorption spectra of the heme-bound and ZnPPIX-bound protein forms. Furthermore, we report the NMR backbone and side-chain resonance assignments (1H, 13C, 15N) of the complex, as well as the chemical shift-based secondary structure predictions. These data will be used for comparative analysis of 15N NMR relaxation experiments in the basal, fully active and inactive H-NOX states, aiming to elucidate the role of Η-ΝΟΧ protein dynamics in the initiation and propagation of sGC activation signal.</div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"20 1","pages":""},"PeriodicalIF":0.5,"publicationDate":"2026-08-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s12104-026-10274-5.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148817014","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, 15N and 13C backbone and side-chain resonance assignments of Amblyomin-X Kunitz domain Amblyomin-X Kunitz结构域的1H， 15N和13C主链和侧链共振分配。

IF 0.5 4区生物学

Biomolecular NMR Assignments Pub Date : 2026-08-24 DOI: 10.1007/s12104-026-10275-4

Vitor S. Almeida, Virginnia C. Nogueira, Livia S. O. Conti, Ana Paula B. Costa, Ana Paula Valente

{"title":"1H, 15N and 13C backbone and side-chain resonance assignments of Amblyomin-X Kunitz domain","authors":"Vitor S. Almeida, Virginnia C. Nogueira, Livia S. O. Conti, Ana Paula B. Costa, Ana Paula Valente","doi":"10.1007/s12104-026-10275-4","DOIUrl":"10.1007/s12104-026-10275-4","url":null,"abstract":"<div>Amblyomin-X is a Kunitz-type inhibitor of factor Xa (FXa) from the tick Amblyomma sculptum with promising anticoagulant activity and potential therapeutic applications. Despite the relevance, the molecular basis of its interaction with FXa remains poorly understood, limiting a detailed understanding of its mechanism of action. In this study, we report the 1H, 13C, and 15N resonance assignments of the Amblyomin-X Kunitz domain obtained by multidimensional NMR spectroscopy. High-quality spectra enabled extensive assignment, reaching 97.9% completeness for backbone assignments and 79.8% for side-chain assignments. The 1H-15N HSQC spectrum shows excellent signal dispersion, consistent with a well-folded protein in solution. Furthermore, chemical shift-based structure analysis reveals elements that agree with the canonical Kunitz fold, including characteristic β-strands and helical regions. These results provide the first detailed NMR characterization of the Amblyomin-X Kunitz domain l. The resonance assignments presented here constitute a critical foundation for future structural and dynamical studies, including analyses of protein-ligand interactions. Ultimately, this work contributes to a deeper understanding of the molecular determinants governing FXa inhibition by Amblyomin-X and supports ongoing efforts to develop novel anticoagulant strategies based on Kunitz-type inhibitors.</div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"20 1","pages":""},"PeriodicalIF":0.5,"publicationDate":"2026-08-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13503397/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148811778","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