Selected article for: "Î hairpin and Î strand helix"
Author: Dene Littler; Benjamin Gully; Rhys N Colson; Jamie Rossjohn
Title: Crystal structure of the SARS-CoV-2 non-structural protein 9, Nsp9
  • Document date: 2020_3_30
    • ID: beoseizn_14
    Snippet: . CC-BY-ND 4.0 International license author/funder. It is made available under a The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.03.28.013920 doi: bioRxiv preprint components of the dimer interface (Fig. 3A) . Two loops project from the open-face of the barrel: the β2-3-and β3-4-loops are both positively charged, glycine rich, and are proposed to be involved in RNA-binding. The only pro.....
    Document: . CC-BY-ND 4.0 International license author/funder. It is made available under a The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.03.28.013920 doi: bioRxiv preprint components of the dimer interface (Fig. 3A) . Two loops project from the open-face of the barrel: the β2-3-and β3-4-loops are both positively charged, glycine rich, and are proposed to be involved in RNA-binding. The only protrusion on the enclosed barrel-side is the β6-7-loop; the Cterminal half of the β7-strand is an integral part of the fold's barrel-core but its other half extended outward to pair with the external β6-strand and create a twisted β-hairpin, cupping the α1-helix and interacting with subsequent C-terminal residues.

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