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UnknownNMR structures of three single-residue variants of the human prion protein.
The NMR structures of three single-amino acid variants of the C-terminal domain of the human prion protein, hPrP(121-230), are presented. In hPrP(M166V) and hPrP(R220K) the substitution is with the corresponding residue in murine PrP, and in hPrP(S170N) it is with the corresponding Syrian hamster re...
S-EPMC26949 | biostudies-literature
UnknownNMR solution structure of the human prion protein.
The NMR structures of the recombinant human prion protein, hPrP(23-230), and two C-terminal fragments, hPrP(90-230) and hPrP(121-230), include a globular domain extending from residues 125-228, for which a detailed structure was obtained, and an N-terminal flexibly disordered "tail." The globular do...
S-EPMC26630 | biostudies-literature
UnknownPrion protein NMR structures of cats, dogs, pigs, and sheep.
The NMR structures of the recombinant cellular form of the prion proteins (PrPC) of the cat (Felis catus), dog (Canis familiaris), and pig (Sus scrofa), and of two polymorphic forms of the prion protein from sheep (Ovis aries) are presented. In all of these species, PrPC consists of an N-terminal fl...
S-EPMC545531 | biostudies-literature
UnknownA fast, efficient and sequence-independent method for flexible multiple segmental isotope labeling of RNA using ribozyme and RNase H cleavage.
Structural information on RNA, emerging more and more as a major regulator in gene expression, dramatically lags behind compared with information on proteins. Although NMR spectroscopy has proven to be an excellent tool to solve RNA structures, it is hampered by the severe spectral resonances overla...
S-EPMC2978384 | biostudies-literature
UnknownCharacterization of the hcnABC gene cluster encoding hydrogen cyanide synthase and anaerobic regulation by ANR in the strictly aerobic biocontrol agent Pseudomonas fluorescens CHA0.
The secondary metabolite hydrogen cyanide (HCN) is produced by Pseudomonas fluorescens from glycine, essentially under microaerophilic conditions. The genetic basis of HCN synthesis in P. fluorescens CHA0 was investigated. The contiguous structural genes hcnABC encoding HCN synthase were expressed f...
S-EPMC107821 | biostudies-literature
UnknownStructural modeling of protein-RNA complexes using crosslinking of segmentally isotope-labeled RNA and MS/MS.
Ribonucleoproteins (RNPs) are key regulators of cellular function. We established an efficient approach, crosslinking of segmentally isotope-labeled RNA and tandem mass spectrometry (CLIR-MS/MS), to localize protein-RNA interactions simultaneously at amino acid and nucleotide resolution. The approac...
S-EPMC5505470 | biostudies-literature
UnknownThe solution structure of Dead End bound to AU-rich RNA reveals an unusual mode of tandem RRM-RNA recognition required for mRNA regulation.
Dead End (DND1) is an RNA-binding protein essential for germline development through its role in post-transcriptional gene regulation. The molecular mechanisms behind selection and regulation of its targets are unknown. Here, we present the solution structure of DND1's tandem RNA Recognition Motifs ...
S-EPMC9537309 | biostudies-literature
UnknownAberrant interaction of FUS with the U1 snRNA provides a molecular mechanism of FUS induced amyotrophic lateral sclerosis.
Mutations in the RNA-binding protein Fused in Sarcoma (FUS) cause early-onset amyotrophic lateral sclerosis (ALS). However, a detailed understanding of central RNA targets of FUS and their implications for disease remain elusive. Here, we use a unique blend of crosslinking and immunoprecipitation (C...
S-EPMC7733473 | biostudies-literature
ProteomicsHEK293T LC-MSMS of DND1 immunoprecipitations
HEK293T interactomes of transiently expressed RNA-binding protein DND1: WT (replicates P9-1, P10-1, P18-1), R98A RNA binding mutant (replicates P9-2, P10-2, P18-2) and 1-235 dsRBD truncation mutant (replicates P9-3, P10-3, P18-3)
ORGANISM(S): Homo sapiens (Human) 
2022-05-30 | PXD024666 | Pride
Human Lc-msms Dnd1 Hek293t 
ProteomicsHybrid structural modeling of protein-RNA complexes using crosslinking of segmentally isotope labeled RNA and tandem mass spectrometry
To study protein-RNA interactions at single amino acid and single nucleotide resolution we developed a new approach, termed cross-linking of segmentally isotope labeled RNA and tandem mass spectrometry (CLIR-MS/MS). The method was developed using the PTBP1-EMCV IRES complex as a model system and add...
ORGANISM(S): Homo sapiens (Human) 
2017-03-27 | PXD005566 | Pride
Photochemical cross-linking  protein-rna cross-linking  segmental isotope labeling of rna  clir-ms/ms  ribonucleoproteins  structural proteomics  polypyrimidine tract binding protein 1  u1 snrnp 
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