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2rnk

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

    Title Nuclear magnetic resonance structure shows that the severe acute respiratory syndrome coronavirus-unique domain contains a macrodomain fold. J.Virol. 83 1823-1836 2009
    Site JCSG
    PDB Id 2rnk Target Id
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    Related PDB Ids 2jzf 
    Molecular Characteristics
    Source
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    Alias Ids
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    TPS9380,29837497
    Molecular Weight
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    Da.
    Residues
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    Isoelectric Point
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    Sequence
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      BLAST   FFAS

    Structure Determination
    Method NMR
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    Chains 1

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 2rnk
    1. Nuclear magnetic resonance structure shows that the severe acute respiratory syndrome coronavirus-unique domain contains a macrodomain fold
    A Chatterjee, MA Johnson, P Serrano, B Pedrini - Journal of , 2009 - Am Soc Microbiol
     

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    Protein Summary

    The nuclear magnetic resonance (NMR) structure of a central segment of the previously annotated severe acute respiratory syndrome (SARS)-unique domain (SUD-M, for "middle of the SARS-unique domain") in SARS coronavirus (SARS-CoV) nonstructural protein 3 (nsp3) has been determined. SUD-M(513-651) exhibits a macrodomain fold containing the nsp3 residues 528 to 648, and there is a flexibly extended N-terminal tail with the residues 513 to 527 and a C-terminal flexible tail of residues 649 to 651. As a follow-up to this initial result, we also solved the structure of a construct representing only the globular domain of residues 527 to 651 [SUD-M(527-651)]. This domain belongs to the Nsp3 family (PF11633). NMR chemical shift perturbation experiments showed that SUD-M(527-651) binds single-stranded poly(A) and identified the contact area with this RNA on the protein surface, and electrophoretic mobility shift assays then confirmed that SUD-M has higher affinity for purine bases than for pyrimidine bases. In a further search for clues to the function, we found that SUD-M(527-651) has the closest three-dimensional structure homology with another domain of nsp3, the ADP-ribose-1"-phosphatase nsp3b (PDB_ID: 3EWQ; Z=10), although the two proteins share only 5% sequence identity in the homologous sequence regions. SUD-M(527-651) also shows three-dimensional structure homology with several helicases and nucleoside triphosphate-binding proteins (3KH6; Z=8), but it does not contain the motifs of catalytic residues found in these structural homologues. The combined results from NMR screening of potential substrates and the structure-based homology studies now form a basis for more focused investigations on the role of the SARS-unique domain in viral infection.

    Ligand Summary

    Reviews

    References

     

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