|Journal of Virology (2007) 81(21):12049-60|
|Joint Center for Structural Genomics|
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This paper describes the structure determination of nsp3a, the N-terminal domain of the severe acute respiratory syndrome coronavirus (SARS-CoV) nonstructural protein 3. ...
nsp3a exhibits a ubiquitin-like globular fold of residues 1 to 112 and a flexibly extended glutamic acid-rich domain of residues 113 to 183. 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 feature that has not previously been observed in these proteins. Nuclear magnetic resonance chemical shift perturbations showed that these unique structural elements are involved in interactions with single-stranded RNA. Structural similarities with proteins involved in various cell-signaling pathways indicate possible roles of nsp3a in viral infection and persistence.
|metabolism chemistry methods |
|Protein Structure, Tertiary Amino Acid Sequence Models, Molecular Molecular Sequence Data Protein Structure, Secondary Mass Spectrometry Molecular Conformation Protein Conformation Sequence Homology, Amino Acid Dose-Response Relationship, Drug Magnetic Resonance Spectroscopy Viral Proteins RNA, Viral RNA Replicase SARS Virus Viral Nonstructural Proteins |
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