Solution-state NMR articles within Nature

Featured

  • Article |

    Systematic alteration of HIV-1 TAR RNA and quantitative determination of its propensity to bind to the Tat protein establish a key role role for a rare and short-lived RNA state in Tat-dependent transactivation in cells.

    • Megan L. Ken
    • , Rohit Roy
    •  & Hashim M. Al-Hashimi
  • Article |

    Combining NMR spectroscopy-derived pseudocontact shifts (PCSs) with Carr–Purcell–Meiboom–Gill (CPMG) relaxation dispersion enables protein structure determination of lowly populated high-energy states that are essential for macromolecular function.

    • John B. Stiller
    • , Renee Otten
    •  & Dorothee Kern
  • Article |

    Repression of a messenger RNA by a cognate microRNA depends not only on complementary base pairing, but also on the rearrangement of a single base pair, producing a conformation that fits better within the human Ago2 protein.

    • Lorenzo Baronti
    • , Ileana Guzzetti
    •  & Katja Petzold
  • Article |

    Chaperones interact with a canonical motif in α-synuclein, which can be prevented by phosphorylation of α-synuclein at Tyr39, whereas inhibition of this interaction leads to the localization of α-synuclein to the mitochondria and aggregate formation.

    • Björn M. Burmann
    • , Juan A. Gerez
    •  & Sebastian Hiller
  • Article |

    A high-affinity complex of histone H1 and prothymosin-α reveals an unexpected interaction mechanism, where the large opposite net charge enables the two proteins to remain highly disordered even in the complex.

    • Alessandro Borgia
    • , Madeleine B. Borgia
    •  & Benjamin Schuler
  • Letter |

    The intrinsically disordered CITED2 negative feedback regulator displaces the tightly bound hypoxia-inducible transcription factor HIF-1α from their common target TAZ1 through the formation of an intermediate ternary complex and thereby attenuates the hypoxic response.

    • Rebecca B. Berlow
    • , H. Jane Dyson
    •  & Peter E. Wright
  • Letter |

    The structure of the core region of the mitochondrial calcium uniporter (MCU) is determined by NMR and electron microscopy, revealing that MCU is a homo-pentamer with a specific transmembrane helix forming a hydrophilic pore across the membrane, and representing one of the largest membrane protein structures characterized by NMR spectroscopy.

    • Kirill Oxenoid
    • , Ying Dong
    •  & James J. Chou
  • Letter |

    Although several X-ray crystal structures of G protein-coupled receptors (GPCRs) have been reported, relatively little is known about the conformational dynamics of these important membrane proteins; here, the authors used NMR spectroscopy to monitor the conformational changes that occur in the turkey β1-adrenergic receptor in the presence of antagonists, partial agonists, and full agonists.

    • Shin Isogai
    • , Xavier Deupi
    •  & Stephan Grzesiek
  • Article |

    Atomic resolution in-cell NMR and EPR spectroscopy show that the human amyloid protein α-synuclein remains disordered within all mammalian cells tested, including neurons, and identifies which parts of the protein dynamically interact or remain shielded from the cytoplasm, thus counteracting aggregation under physiological cell conditions.

    • Francois-Xavier Theillet
    • , Andres Binolfi
    •  & Philipp Selenko
  • Letter |

    NMR spectroscopy reveals the conformational changes of the μ-opioid receptor that are associated with receptor activation, helping to explain why the allosteric coupling between the agonist-binding pocket and the cytoplasmic G-protein-coupling interface of this receptor is relatively weak.

    • Rémy Sounier
    • , Camille Mas
    •  & Sébastien Granier
  • Article |

    dG•dT and rG•rU ‘wobble’ mispairs in DNA and RNA transiently form base pairs with Watson–Crick geometry via tautomerization and ionization with probabilities that correlate with misincorporation probabilities during replication and translation.

    • Isaac J. Kimsey
    • , Katja Petzold
    •  & Hashim M. Al-Hashimi
  • Letter |

    To prime reverse transcription of Moloney murine leukaemia virus, a transfer RNA molecule must bind two regions of the retroviral RNA, the primer binding site (PBS) and primer activation signal within the U5-PBS; here, the NMR structures of the U5-PBS RNA and tRNA primer are solved, with and without the retroviral nucleocapsid protein, which remodels these regions.

    • Sarah B. Miller
    • , F. Zehra Yildiz
    •  & Victoria M. D’Souza
  • Article |

    RNAs undergo many types of post-transcriptional modification, including methylation of ribosomal RNAs; here the structure of the archaeal box C/D ribonucleoprotein complex bound to substrate RNA is determined, showing that the two methylation guide sequences exist in different contexts and revealing sequential regulation of methylation at the two sites.

    • Audrone Lapinaite
    • , Bernd Simon
    •  & Teresa Carlomagno
  • Letter |

    The structure of the oligomeric hepatitis C virus viroporin p7 protein, solved by NMR spectroscopy, is reported; this protein can self-assemble into a channel complex that conducts cations and has a funnel-like channel architecture.

    • Bo OuYang
    • , Shiqi Xie
    •  & James J. Chou