Selected article for: "Ã resolution and crystal structure"

Author: Rajanish Giri; Taniya Bhardwaj; Meenakshi Shegane; Bhuvaneshwari R. Gehi; Prateek Kumar; Kundlik Gadhave
Title: Dark Proteome of Newly Emerged SARS-CoV-2 in Comparison with Human and Bat Coronaviruses
  • Document date: 2020_3_14
  • ID: n7ylgqfu_53
    Snippet: This protein is expressed from an alternative ORF within the N gene through a leaky ribosome binding process [119] . Inside the host cells, ORF9b enters the nucleus, which is a cell cycle-independent process and represents a passive entry. This protein was shown to interact with a nuclear export protein receptor Exportin 1 (Crm1), using which it translocate out of the nucleus [120] . Our MoRFs analysis shows the presence of disorderbased protein .....
    Document: This protein is expressed from an alternative ORF within the N gene through a leaky ribosome binding process [119] . Inside the host cells, ORF9b enters the nucleus, which is a cell cycle-independent process and represents a passive entry. This protein was shown to interact with a nuclear export protein receptor Exportin 1 (Crm1), using which it translocate out of the nucleus [120] . Our MoRFs analysis shows the presence of disorderbased protein binding regions in ORF9b protein which may have role in its interaction with Crm1 and further translocation outside the nucleus. A 2.8 Ã… resolution crystal structure of ORF9b protein from Human SARS CoV (PDB ID: 2CME) shows the presence of a dimeric tent-like -structure along with the central hydrophobic amino acids (Figure 14D) . The author/funder. All rights reserved. No reuse allowed without permission.

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