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TitleAromatic Interactions Drive the Coupled Folding and Binding of the Intrinsically Disordered Sesbania mosaic Virus VPg Protein.
Journal, issue, pagesBiochemistry, Vol. 59, Page 4663-4680, Year 2020
Publish dateFeb 11, 2020 (structure data deposition date)
AuthorsDixit, K. / Karanth, N.M. / Nair, S. / Kumari, K. / Chakrabarti, K.S. / Savithri, H.S. / Sarma, S.P.
External linksBiochemistry / PubMed:33269926
MethodsNMR (solution)
Structure data

PDB-6lxf:
Aromatic interactions drive the coupled folding and binding of the intrinsically disordered Sesbania mosaic virus VPg protein.
Method: SOLUTION NMR

PDB-6m78:
Aromatic interactions drive the coupled folding and binding of the intrinsically disordered Sesbania mosaic virus VPg protein
Method: SOLUTION NMR

Source
  • sesbania mosaic virus
KeywordsPLANT VIRAL PROTEIN / IDPs (Intrinsically Disorder Proteins) / VPg (Viral Protein genome linked) / HYDROLASE / Viral-Protein-genome-linked / complex / protease

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