Biomolecular NMR Assignments

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Backbone assignment of crystalline E. coli maltose binding protein
Biomolecular NMR Assignments - Tập 15 - Trang 317-322 - 2021
Tobias Schubeis, Jan Stanek, Guido Pintacuda
The E.coli maltose binding protein (MBP) is a 42.5 kDa molecule widely employed in many biotechnology applications. Because of its molecular size, it has become the main model system for the development of solution NMR methods adapted to large biomolecular targets. Here, we report virtually complete (~ 90%) backbone resonance assignments obtained on a microcrystalline sample of MBP with 1H-detected solid-state NMR at fast (> 100 kHz) magic-angle spinning. We additionally present the detailed description of the methodology employed for the preparation of the sample and the acquisition and analysis of the NMR spectra. The chemical shifts, obtained with a single uniformly 15N, 13C-labelled and fully-protonated sample and about 2 weeks on a 800 MHz NMR spectrometer, have been deposited to the BMRB under the accession number 50089.
Backbone NMR assignment of the internal interaction site of ALP
Biomolecular NMR Assignments - Tập 1 Số 1 - Trang 85-87 - 2007
Nanna Alho, Tuula Klaavuniemi, Jari Ylänne, Perttu Permi, Sampo Mattila
1H, 13C, 15N Backbone and sidechain chemical shift assignments of the C-terminal domain of human UDP-glucuronosyltransferase 2B17 (UGT2B17-C)
Biomolecular NMR Assignments - Tập 17 - Trang 67-73 - 2023
Anamika Sulekha, Michael J. Osborne, Jadwiga Gasiorek, Katherine L. B. Borden
UDP-glucuronosyltransferases are the principal enzymes involved in the glucuronidation of metabolites and xenobiotics for physiological clearance in humans. Though glucuronidation is an indispensable process in the phase II metabolic pathway, UGT-mediated glucuronidation of most prescribed drugs (> 55%) and clinical evidence of UGT-associated drug resistance are major concerns for therapeutic development. While UGTs are highly conserved enzymes, they manifest unique substrate and inhibitor specificity which is poorly understood given the dearth of experimentally determined full-length structures. Such information is important not only to conceptualize their specificity but is central to the design of inhibitors specific to a given UGT in order to avoid toxicity associated with pan-UGT inhibitors. Here, we provide the 1H, 13C and 15N backbone (~ 90%) and sidechain (~ 62%) assignments for the C-terminal domain of UGT2B17, which can be used to determine the molecular binding sites of inhibitor and substrate, and to understand the atomic basis for inhibitor selectivity between UGT2B17 and other members of the UGT2B subfamily. Given the physiological relevance of UGT2B17 in the elimination of hormone-based cancer drugs, these assignments will contribute towards dissecting the structural basis for substrate specificity, selective inhibitor recognition and other aspects of enzyme activity with the goal of selectively overcoming glucuronidation-based drug resistance.
1H, 13C and 15N resonances of the AlgE62 subunit from Azotobacter vinelandii mannuronan C5-epimerase
Biomolecular NMR Assignments - Tập 5 - Trang 147-149 - 2010
Trygve Andreassen, Edith Buchinger, Gudmund Skjåk-Bræk, Svein Valla, Finn L. Aachmann
The 17.7 kDa R2 module from Azotobacter vinelandii mannronan C5-epimerase AlgE6 has been isotopically labeled (13C,15N) and recombinantly expressed. Here we report the 1H, 13C, 15N resonance assignment of AlgE6R2.
The 1H, 15N, and 13C resonance assignments of the N-terminal domain of the nucleocapsid protein from the Middle East respiratory syndrome coronavirus
Biomolecular NMR Assignments - Tập 15 - Trang 341-345 - 2021
Talita Stelling de Araujo, Glauce Moreno Barbosa, Karoline Sanches, Jéssica M. Azevedo, Katia Maria dos Santos Cabral, Marcius S. Almeida, Fabio C. L. Almeida
During the past 17 years, the coronaviruses have become a global public emergency, with the first appearance in 2012 in Saudi Arabia of the Middle East respiratory syndrome. Among the structural proteins encoded in the viral genome, the nucleocapsid protein is the most abundant in infected cells. It is a multifunctional phosphoprotein involved in the capsid formation, in the modulation and regulation of the viral life cycle. The N-terminal domain of N protein specifically interacts with transcriptional regulatory sequence (TRS) and is involved in the discontinuous transcription through the melting activity of double-stranded TRS (dsTRS).
13C and 15N chemical shift assignments and secondary structure of the B3 immunoglobulin-binding domain of streptococcal protein G by magic-angle spinning solid-state NMR spectroscopy
Biomolecular NMR Assignments - Tập 1 - Trang 117-120 - 2007
Philippe S. Nadaud, Jonathan J. Helmus, Christopher P. Jaroniec
Complete 13C and 15N assignments of the B3 IgG-binding domain of protein G (GB3) in the microcrystalline solid phase, obtained using 2D and 3D MAS NMR, are presented. The chemical shifts are used to predict the protein backbone conformation and compared with solution-state shifts.
A complete backbone spectral assignment of lipid-free human apolipoprotein E (apoE)
Biomolecular NMR Assignments - Tập 2 - Trang 207-210 - 2008
Yonghong Zhang, Jianglei Chen, Jianjun Wang
Apolipoprotein E is an exchangeable apolipoprotein that plays an important role in lipid/lipoprotein metabolism and cardiovascular diseases. Recent evidence indicates that apoE is also critical in several other important biological processes, including Alzheimer’s disease, cognitive function, immunoregulation, cell signaling and infectious diseases. Although the X-ray crystal structure of the apoE N-terminal domain was solved in 1991, there is no structure available for the apoE C-terminal domain and full-length apoE. Here we report a complete NMR backbone spectral assignment of lipid-free human apoE.
NMR assignments of juvenile hormone binding protein in complex with JH III
Biomolecular NMR Assignments - Tập 3 - Trang 73-76 - 2009
Rintaro Suzuki, Akira Tase, Zui Fujimoto, Takahiro Shiotsuki, Toshimasa Yamazaki
A hemolymph juvenile hormone binding protein (JHBP) shuttles hydrophobic JH, a key hormone in regulation of the insect life cycle, from the site of the JH biosynthesis to the cells of target organs. We report complete NMR chemical shift assignments of Bombyx mori JHBP in the JH III-bound state.
Assignment of Ala, Ile, LeuproS, Met, and ValproS methyl groups of the protruding domain of murine norovirus capsid protein VP1 using methyl–methyl NOEs, site directed mutagenesis, and pseudocontact shifts
Biomolecular NMR Assignments - Tập 16 - Trang 97-107 - 2022
Thorben Maass, Leon Torben Westermann, Robert Creutznacher, Alvaro Mallagaray, Jasmin Dülfer, Charlotte Uetrecht, Thomas Peters
The protruding domain (P-domain) of the murine norovirus (MNV) capsid protein VP1 is essential for infection. It mediates receptor binding and attachment of neutralizing antibodies. Protein NMR studies into interactions of the P-domain with ligands will yield insights not easily available from other biophysical techniques and will extend our understanding of MNV attachment to host cells. Such studies require at least partial NMR assignments. Here, we describe the assignment of about 70% of the Ala, Ile, LeuproS, Met, and ValproS methyl groups. An unfavorable distribution of methyl group resonance signals prevents complete assignment based exclusively on 4D HMQC-NOESY-HMQC experiments, yielding assignment of only 55 out of 100 methyl groups. Therefore, we created point mutants and measured pseudo contact shifts, extending and validating assignments based on methyl-methyl NOEs. Of note, the P-domains are present in two different forms caused by an approximate equal distribution of trans- and cis-configured proline residues in position 361.
1H, 13C and 15N backbone NMR chemical shift assignments of the C-terminal P4 domain of Ahnak
Biomolecular NMR Assignments - Tập 12 Số 2 - Trang 253-257 - 2018
Srinivasan Sundararaj, Dmitry Shishmarev, Yiechang Lin, Shouvik Aditya, Marco G. Casarotto
Tổng số: 792   
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