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Assignment of the N-terminal domain of mouse cGAS.
Biomol NMR Assign
January 2025
Department of Chemistry and Chemical Biology, TU Dortmund University, Dortmund, Germany.
Cyclic GMP-AMP synthase (cGAS) is a DNA-sensing enzyme that is a member of the nucleotidyltransferase (NTase) family and functions as a DNA sensor. The protein is comprised of a catalytic NTase core domain and an unstructured hypervariable N-terminal domain (NTD) that was reported to increase protein activity by providing an additional DNA-binding surface. We report nearly complete H, N, and C backbone chemical-shift assignments of mouse cGAS NTD (residues 5-146), obtained with a set of 3D and 4D solution NMR experiments.
View Article and Find Full Text PDFBackbone NMR resonance assignment of Sis1, a type B J-domain protein from Saccharomyces cerevisiae.
Biomol NMR Assign
December 2024
Institute of Medical Biochemistry, Federal University of Rio de Janeiro, Rio de Janeiro, RJ, Brazil.
J-domain proteins (JDPs) are essential cochaperones of heat shock protein 70 (Hsp70), as they bind and deliver misfolded polypeptides while also stimulating ATPase activity, thereby mediating the refolding process and assisting Hsp70 in maintaining cellular proteostasis. Despite their importance, detailed structural information about JDP‒Hsp70 complexes is still being explored due to various technical challenges. One major challenge is the lack of more detailed structural data on full-length JDPs.
View Article and Find Full Text PDFMolecular dynamics as an efficient process to predict N chemical shift anisotropy at very high NMR magnetic fields.
Phys Chem Chem Phys
December 2024
Universite de Lyon, CNRS, UCB Lyon1, Institut des Sciences Analytiques, UMR5280, Villeurbanne, France.
The emergence of very high NMR magnetic fields will certainly encourage the study of larger biological systems with their dynamics and interactions. NMR spin relaxation allows probing the dynamical properties of proteins where the N longitudinal () and transverse () relaxation rates in addition to the H-N heteronuclear NOE describe the ps-ns time scale. Their analytical representation involves the chemical shift anisotropy (CSA) effect that represents the major contribution at a very high magnetic field above 18.
View Article and Find Full Text PDFDynamic conformational equilibria in the active states of KRAS and NRAS.
RSC Chem Biol
January 2025
Novartis Biomedical Research Basel Switzerland
The design of potent RAS inhibitors benefits from a molecular understanding of the dynamics in KRAS and NRAS and their oncogenic mutants. Here we characterize switch-1 dynamics in GTP-state KRAS and NRAS by P NMR, by N relaxation dispersion NMR, hydrogen-deuterium exchange mass spectrometry (HDX-MS), and molecular dynamics simulations. In GMPPNP-bound KRAS and NRAS, we see the co-existence of two conformational states, corresponding to an "inactive" state-1 and an "active" state-2, as previously reported.
View Article and Find Full Text PDFH, C, and N resonance assignments of the amyloidogenic peptide SEM2(49-107) by NMR spectroscopy.
Biomol NMR Assign
November 2024
NMR Laboratory, Medical Physics Department, Institute of Physics, Kazan Federal University, Kremlevskaya Str., 18, Kazan, 420008, Russia.
It has been shown that human seminal fluid is a major factor in enhancing HIV activity. The SEM2(49-107) peptide is a product of cleavage after ejaculation by internal prostheses of the semenogelin 2 protein, expressed in seminal vesicles. It is established that the peptide SEM2(49-107) forms amyloid fibrils, which increase probability of contracting HIV infection.
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