Proteins

Proteins are biopolymers of amino acids (polypeptides), joined by peptide bonds, that are generated by ribosomes. The amino acid sequence, encoded by its gene, determines a protein’s structure and function. Newly synthesized proteins can be modified by post-translational modification, altering its protein folding, stability and activity. Proteins often associate into protein–protein interaction networks for function.

Latest Research and Reviews

  • Research |

    A strategy using droplet-based and barcode-linked sequencing captures multiplex chromatin interactions at single-molecule precision, and here provides topological insight into chromatin structures and transcription in Drosophila.

    • Meizhen Zheng
    • , Simon Zhongyuan Tian
    • , Daniel Capurso
    • , Minji Kim
    • , Rahul Maurya
    • , Byoungkoo Lee
    • , Emaly Piecuch
    • , Liang Gong
    • , Jacqueline Jufen Zhu
    • , Zhihui Li
    • , Chee Hong Wong
    • , Chew Yee Ngan
    • , Ping Wang
    • , Xiaoan Ruan
    • , Chia-Lin Wei
    •  & Yijun Ruan
    Nature, 1-5
  • Research | | open

    The main components of tight junctions (TJ) are claudins that polymerize and form meshwork architectures called TJ strands. Here the authors present the 3.6 Å crystal structure of murine claudin-3 and show that residue P134 causes a bending of the third transmembrane helix which affects the morphology and adhesiveness of the TJ strands.

    • Shun Nakamura
    • , Katsumasa Irie
    • , Hiroo Tanaka
    • , Kouki Nishikawa
    • , Hiroshi Suzuki
    • , Yasunori Saitoh
    • , Atsushi Tamura
    • , Sachiko Tsukita
    •  & Yoshinori Fujiyoshi
  • Research |

    A concise strategy for engineering functional, supramolecular protein complexes has now been developed based on single-mutation-mediated covalent tethering. Metalloproteins designed with this method can sustain large alterations to the metal coordination environment, bind small molecules, exhibit reversible redox activity and sustain large alterations to the protein structure.

    • Jonathan Rittle
    • , Mackenzie J. Field
    • , Michael T. Green
    •  & F. Akif Tezcan
  • Research | | open

    SecB homologs can be associated with stress-responsive type II toxin–antitoxin (TA) systems and form tripartite toxin-antitoxin-chaperone systems (TAC). Here the authors provide structural insights into TACs by presenting the crystal structure of the M. tuberculosis TA-associated SecB chaperone in complex with the C-terminal ChAD (chaperone addiction) extension of the antitoxin HigA1.

    • Valérie Guillet
    • , Patricia Bordes
    • , Cécile Bon
    • , Julien Marcoux
    • , Virginie Gervais
    • , Ambre Julie Sala
    • , Suzana Dos Reis
    • , Nawel Slama
    • , Israel Mares-Mejía
    • , Anne-Marie Cirinesi
    • , Laurent Maveyraud
    • , Pierre Genevaux
    •  & Lionel Mourey

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