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TitleTargeting the N-Terminus Domain of the Coronavirus Nucleocapsid Protein Induces Abnormal Oligomerization via Allosteric Modulation.
Journal, issue, pagesFront Mol Biosci, Vol. 9, Page 871499-871499, Year 2022
Publish dateDec 31, 2019 (structure data deposition date)
AuthorsHsu, J.N. / Chen, J.S. / Lin, S.M. / Hong, J.Y. / Chen, Y.J. / Jeng, U.S. / Luo, S.Y. / Hou, M.H.
External linksFront Mol Biosci / PubMed:35517857
MethodsX-ray diffraction
Resolution2.39 - 2.646 Å
Structure data

PDB-6lnn:
Crystal structure of MERS-CoV N-NTD complexed with ligand P4-1
Method: X-RAY DIFFRACTION / Resolution: 2.634 Å

PDB-6lz6:
Crystal structure of MERS-CoV N-NTD complexed with ligand P4-3
Method: X-RAY DIFFRACTION / Resolution: 2.646 Å

PDB-6lz8:
Crystal structure of MERS-CoV N-NTD complexed with ligand P4-4
Method: X-RAY DIFFRACTION / Resolution: 2.59 Å

PDB-7dyd:
Crystal structure of MERS-CoV N-NTD complexed with ligand P4-2
Method: X-RAY DIFFRACTION / Resolution: 2.39 Å

Chemicals

ChemComp-EJC:
5-propoxy-1H-indole

ChemComp-HOH:
WATER

ChemComp-EY6:
5-(2-fluoranylethoxy)-1H-indole

ChemComp-EY9:
5-(2-methoxyethoxy)-1H-indole

ChemComp-EY3:
5-propan-2-yloxy-1H-indole

Source
  • middle east respiratory syndrome-related coronavirus
KeywordsVIRAL PROTEIN / Middle East respiratory syndrome coronavirus / nucleocapsid protein / N-terminal domain

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