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TitleSolution structures of Mengovirus Leader protein, its phosphorylated derivatives, and in complex with nuclear transport regulatory protein, RanGTPase.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 111, Page 15792-15797, Year 2014
Publish dateMar 15, 2014 (structure data deposition date)
AuthorsBacot-Davis, V.R. / Ciomperlik, J.J. / Basta, H.A. / Cornilescu, C.C. / Palmenberg, A.C.
External linksProc. Natl. Acad. Sci. USA / PubMed:25331866
MethodsNMR (solution)
Structure data

PDB-2mmg:
Structural Characterization of the Mengovirus Leader Protein Bound to Ran GTPase by Nuclear Magnetic Resonance
Method: SOLUTION NMR

PDB-2mmh:
Unphosphorylated Mengovirus Leader Protein: NMR Studies of the Phosphorylation of the Mengovirus Leader Protein Reveal Stabilization of Intermolecular Domain Interactions
Method: SOLUTION NMR

PDB-2mmi:
Mengovirus Leader: Structural Characterization of the Mengovirus Leader Protein Bound to Ran GTPase by Nuclear Magnetic Resonance
Method: SOLUTION NMR

PDB-2mmk:
Y41 and T47 phosphorylation of the Mengovirus Leader Protein: NMR Studies of the Phosphorylation of the Mengovirus Leader Protein Reveal Stabilization of Intermolecular Domain Interactions
Method: SOLUTION NMR

PDB-2mml:
T47 phosphorylation of the Mengovirus Leader Protein: NMR Studies of the Phosphorylation of the Mengovirus Leader Protein Reveal Stabilization of Intermolecular Domain Interactions
Method: SOLUTION NMR

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
  • mengo virus
KeywordsTRANSPORT PROTEIN / G-protein / nucleotide binding / GTP binding / virus-host interactions / GTPase / nuclear pore complex / leader / cardioviruses / nucleocytoplasmic transport / nucleus / VIRAL PROTEIN / animal viruses / positive-strand RNA viruses / L / protein phosphorylation / casein kinase 2 / spleen tyrosine kinase

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