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    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary
    3. 3. References

    Title Novel beta-barrel fold in the nuclear magnetic resonance structure of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus. J.Virol. 81 3151-3161 2007
    Site JCSG
    PDB Id 2hsx Target Id 367632
    Related PDB Ids 2gdt 
    Molecular Characteristics
    Source Sars coronavirus
    Alias Ids TPS1518,NP_828860.2 Molecular Weight 12605.87 Da.
    Residues 115 Isoelectric Point 6.21
    Sequence hvqlslpvlqvrdvlvrgfgdsveealsearehlkngtcglvelekgvlpqleqpyvfikrsdalstnh ghkvvelvaemdgiqygrsgitlgvlvphvgetpiayrnvllrkng
      BLAST   FFAS

    Structure Determination
    Method NMR Chains 1

    Ligand Information


    Google Scholar output for 2hsx
    1. Novel _-barrel fold in the nuclear magnetic resonance structure of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus
    MS Almeida, MA Johnson, T Herrmann - Journal of , 2007 - Am Soc Microbiol
    2. Nsp1 proteins of group I and SARS coronaviruses share structural and functional similarities
    Y Wang, H Shi, P Rigolet, N Wu, L Zhu, XG Xi - Infection, Genetics and , 2010 - Elsevier

    Protein Summary

     The gene NP_828860.2 from Sars coronavirus encodes a non-structural protein Nsp1 PF11501.  The protein belongs to the class of alpha and beta (a+b) proteins and adopts a novel SARS Nsp1-like fold[Ref] type SCOP16009. No significant protein functional motifs can be detected in the Nsp1 protein.  Nsp1 is the "leader protein", it is translated from the most 5’ coding region of the SARS-CoV genome.  The conservation of a viral protein indicates its importance in the virus life cycle. The Nsp1 sequence is highly conserved in SARS-CoV isolates sequenced from humans, civet cats and bats, implying that it is crucial to replication of the virus, survival in the host or spread in susceptible populations.  The SARS-CoV Nsp1 is unique among coronaviruses and could contribute to the exceptional pathogenesis of SARS-CoV in humans.  In cells, transfected with Nsp1 RNA, the decrease of host protein synthesis was observed.  The inclusion of actinomycin D (to block new transcription) showed a much stronger inhibition of protein synthesis in the presence of Nsp1. This indicates that while translation of new transcripts was proceeding (in cells not treated with actinomycin D), translation from pre-existing transcripts was blocked by Nsp1. This suggests that Nsp1 increases RNA degradation.  The exact mechanism of its action on RNA is not known. [Ref]

    Ligand Summary





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