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2idy

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

    Title Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirus. J.Virol. 81 12049-12060 2007
    Site JCSG
    PDB Id 2idy Target Id 355891
    Related PDB Ids 2gri 
    Molecular Characteristics
    Source Sars coronavirus tor2
    Alias Ids TPS1353,29837497 Molecular Weight 12639.45 Da.
    Residues 112 Isoelectric Point 4.10
    Sequence apikgvtfgedtvwevqgyknvritfeldervdkvlnekcsvytvesgtevtefacvvaeavvktlqpv sdlltnmgidldewsvatfylfddageenfssrmycsfyppde
      BLAST   FFAS

    Structure Determination
    Method NMR Chains 1

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 2idy
    1. The SARS-unique domain (SUD) of SARS coronavirus contains two macrodomains that bind G-quadruplexes
    J Tan, C Vonrhein, OS Smart, G Bricogne, M Bollati - PLoS , 2009 - dx.plos.org
     
    2. Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirus
    P Serrano, MA Johnson, MS Almeida, R Horst - Journal of , 2007 - Am Soc Microbiol
     
    3. Dimensionality reduction in computational demarcation of protein tertiary structures
    RR Joshi, PR Panigrahi, RN Patil - Journal of Molecular Modeling, 2011 - Springer
     

    Protein Summary

    The gene 29837497 from SARS coronavirus encodes the N-terminal domain of nonstructural protein 3 (nsp3a).  The protein belongs to the class of alpha and beta proteins (a+b) and reveals beta-Grasp (ubiquitine-like) fold type SCOP.  The NMR structure of the same protein has been previously determined 2GRI.  In addition to the four beta-strands and two alpha-helices that are common to ubiquitin-like folds, the globular domain of nsp3a contains two short helices representing a new feature of this protein. NMR chemical shift perturbations showed that these unique structural elements are involved in interactions with single-stranded RNA[Ref].  The nsp3a homologue from rotovirus has been shown to bind to 3'-end of viral mRNA during viral infection [Ref].  While bound to mRNA nsp3a interacts with eukaryotic initiation factor 4GI (eIF4GI), displacing its normal partner PABP.  This interaction effectively shut offs the cellular protein synthesis, dedicating resources to the viral protein synthesis.  Thus, SARS nsp3a seems to have similar function.

    Ligand Summary


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