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Structure paper

TitleContribution of the residue at position 4 within classical nuclear localization signals to modulating interaction with importins and nuclear targeting.
Journal, issue, pagesBiochim Biophys Acta Mol Cell Res, Vol. 1865, Page 1114-1129, Year 2018
Publish dateJun 25, 2016 (structure data deposition date)
AuthorsSmith, K.M. / Di Antonio, V. / Bellucci, L. / Thomas, D.R. / Caporuscio, F. / Ciccarese, F. / Ghassabian, H. / Wagstaff, K.M. / Forwood, J.K. / Jans, D.A. ...Smith, K.M. / Di Antonio, V. / Bellucci, L. / Thomas, D.R. / Caporuscio, F. / Ciccarese, F. / Ghassabian, H. / Wagstaff, K.M. / Forwood, J.K. / Jans, D.A. / Palu, G. / Alvisi, G.
External linksBiochim Biophys Acta Mol Cell Res / PubMed:29750988
MethodsX-ray diffraction
Resolution2.2 - 2.6 Å
Structure data

PDB-5klr:
Prototypical P4[R]cNLS
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-5klt:
Prototypical P4[M]cNLS
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • mus musculus (house mouse)
  • synthetic construct (others)
KeywordsPROTEIN TRANSPORT/Viral protein / Importin alpha / Complex / nuclear localisation signal / PROTEIN TRANSPORT-Viral protein complex

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