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TitleCo-crystal structures of HIV TAR RNA bound to lab-evolved proteins show key roles for arginine relevant to the design of cyclic peptide TAR inhibitors.
Journal, issue, pagesJ. Biol. Chem., Vol. 295, Page 16470-16486, Year 2020
Publish dateJun 18, 2020 (structure data deposition date)
AuthorsChavali, S.S. / Mali, S.M. / Jenkins, J.L. / Fasan, R. / Wedekind, J.E.
External linksJ. Biol. Chem. / PubMed:33051202
MethodsX-ray diffraction
Resolution1.71 - 3.1 Å
Structure data

PDB-6xh0:
Co-crystal structure of HIV-1 TAR RNA in complex with lab-evolved RRM TBP6.9
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

PDB-6xh1:
Co-crystal structure of HIV-1 TAR RNA in complex with lab-evolved RRM TBP6.7 mutant
Method: X-RAY DIFFRACTION / Resolution: 2.601 Å

PDB-6xh2:
Co-crystal structure of HIV-1 TAR RNA in complex with lab-evolved RRM 6.6
Method: X-RAY DIFFRACTION / Resolution: 1.71 Å

PDB-6xh3:
Co-crystal structure of HIV-1 TAR RNA in complex with lab-evolved RRM TBP6.3
Method: X-RAY DIFFRACTION / Resolution: 2.353 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • human immunodeficiency virus 1
KeywordsRNA BINDING PROTEIN/RNA / PROTEIN-RNA COMPLEX / TAR RNA / LAB-EVOLVED PROTEIN / ARGININE FORK / BETA HAIRPIN / MAJOR-GROOVE READOUT / BASE TRIPLE / U1A / HIV-1 / TRANS- ACTIVATION / RNA RECOGNITION MOTIF / RRM / RNA BINDING PROTEIN-RNA COMPLEX / RNA BINDING PROTEIN

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