Selected article for: "active site and catalytic cysteine"

Author: Xufang Deng; Yafang Chen; Anna M. Mielech; Matthew Hackbart; Kristina R. Kesely; Robert C. Mettelman; Amornrat O’Brien; Mackenzie E. Chapman; Andrew D. Mesecar; Susan C. Baker
Title: Structure-Guided Mutagenesis Alters Deubiquitinating Activity and Attenuates Pathogenesis of a Murine Coronavirus
  • Document date: 2019_9_25
  • ID: l3qp0n9f_23
    Snippet: The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. . https://doi.org/10.1101/782409 doi: bioRxiv preprint study are boxed in green. The active site substrate binding loop also involved in binding inhibitors 561 of SARS is shown highlighted in yellow. The sequence alignment was created using ESPript3. The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. were statisticall.....
    Document: The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. . https://doi.org/10.1101/782409 doi: bioRxiv preprint study are boxed in green. The active site substrate binding loop also involved in binding inhibitors 561 of SARS is shown highlighted in yellow. The sequence alignment was created using ESPript3. The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. were statistically analyzed using unpaired t-tests. *, p < 0.05; **, p < 0.01. The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. . https://doi.org/10.1101/782409 doi: bioRxiv preprint . Amino acids are colored by similarity using the RISER coloring scheme. Numbering shown is based on MHV sequence. Amino acids mutated in this study are indicated with a black asterisk, the catalytic cysteine is indicated by a blue asterisk, and those amino acids that bind ubiquitin and were mutated in this study are boxed in green. The active site substrate binding loop also involved in binding inhibitors of SARS is shown highlighted in yellow. The sequence alignment was created using ESPript3.

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