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TitleStructural and calorimetric studies reveal specific determinants for the binding of a high-affinity NLS to mammalian importin-alpha.
Journal, issue, pagesBiochem. J., Vol. 478, Page 2715-2732, Year 2021
Publish dateMar 26, 2020 (structure data deposition date)
Authorsde Oliveira, H.C. / da Silva, T.D. / Salvador, G.H.M. / Moraes, I.R. / Fukuda, C.A. / de Barros, A.C. / Fontes, M.R.M.
External linksBiochem. J. / PubMed:34195786
MethodsX-ray diffraction
Resolution2.15 - 2.663 Å
Structure data

PDB-6wba:
Structure of Mouse Importin alpha MLH1- R470A NLS Peptide Complex
Method: X-RAY DIFFRACTION / Resolution: 2.151 Å

PDB-6wbb:
Structure of Mouse Importin alpha - MLH1-E475A NLS peptide complex
Method: X-RAY DIFFRACTION / Resolution: 2.663 Å

PDB-6wbc:
Structure of Mouse Importin alpha- MLH1-R472K NLS Peptide Complex
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

PDB-7m60:
Structure of Mouse Importin alpha MLH1-S467A NLS Peptide Complex
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • mus musculus (house mouse)
  • homo sapiens (human)
KeywordsPROTEIN TRANSPORT/NUCLEAR PROTEIN / Importin alpha / Nuclear Import / NLS / MLH1 / PROTEIN TRANSPORT / PROTEIN TRANSPORT-NUCLEAR PROTEIN complex / TRANSPORT PROTEIN

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