Browse our June issue

Latest Research

  • Article |

    The structural basis for self-assembly of human SYCP1, the core architectural element of the meiotic synaptonemal complex, reveals an obligate tetrameric structure that assembles into a zipper-like supramolecular lattice.

    • James M. Dunce
    • , Orla M. Dunne
    • , Matthew Ratcliff
    • , Claudia Millán
    • , Suzanne Madgwick
    • , Isabel Usón
    •  & Owen R. Davies
  • Analysis |

    Analysis of 18 available structures and other data reveals a new, conserved structural motif in arrestins and suggests that different phosphorylation patterns of the GPCR C terminus can drive distinct arrestin conformations and functional outcomes.

    • Andrija Sente
    • , Raphael Peer
    • , Ashish Srivastava
    • , Mithu Baidya
    • , Arthur M. Lesk
    • , Santhanam Balaji
    • , Arun K. Shukla
    • , M. Madan Babu
    •  & Tilman Flock
  • Article |

    A cryo-EM structure of the human SLC1 transporter ASCT2 in the inward-facing conformation reveals the retrovirus-docking site and helps to elucidate the transport cycle. The transport domain is more solvent exposed than in most of the homolog structures.

    • Alisa A. Garaeva
    • , Gert T. Oostergetel
    • , Cornelius Gati
    • , Albert Guskov
    • , Cristina Paulino
    •  & Dirk J. Slotboom

News & Comment

  • News & Views |

    Activation signals from GPCRs, the largest receptor family, are transmitted to heterotrimeric G proteins and arrestins, and can be differentially modulated by GPCR phosphorylation. In a recent article, available data, including multiple arrestin structures, are analyzed to decipher common and state-specific conformational changes in arrestins and how these depend on patterns of receptor phosphorylation.

    • Christopher J. Draper-Joyce
    •  & Arthur Christopoulos
  • News & Views |

    Traditional approaches to covalent drug design postulate that noncovalent binding affinity (Ki) should be in the nanomolar range for the lead compound to be attractive. A study by Hansen et al. suggests that covalent K-Ras inhibitors can have weak noncovalent binding affinity yet have fast chemical reactivity (kinact), because K-Ras enhances the covalent reactivity of bound inhibitor, similarly to how enzymes activate their substrates.

    • Alexander V. Statsyuk
  • News & Views |

    Recent developments in transcriptome-wide sequencing technologies have enabled the identification of cellular mRNA decay intermediates. Although canonical mRNA decay has been shown to occur by deadenylation followed by decapping and subsequent exonucleolytic decay from both mRNA ends, a study by Mourelatos and colleagues now defines mRNA fragments that are generated on polysomes by endonucleolytic cleavages phased by the associated ribosome.

    • Tatsuaki Kurosaki
    •  & Lynne E. Maquat
  • News & Views |

    Nanobodies have emerged as highly versatile and useful binding molecules in biomedical research. A technical report describes a cost- and time-effective in vitro platform that facilitates the generation of desired nanobodies, including conformationally selective nanobodies against agonist-bound G-protein-coupled receptors (GPCRs).

    • Ulrich Rothbauer



We mark the 25th year of NSMB with a special Series of commissioned Reviews and Comments that celebrate exciting research uncovering the fundamental principles behind biological processes.