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-Structure paper
Title | Co-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. |
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Journal, issue, pages | J. Biol. Chem., Vol. 295, Page 16470-16486, Year 2020 |
Publish date | Jun 18, 2020 (structure data deposition date) |
![]() | Chavali, S.S. / Mali, S.M. / Jenkins, J.L. / Fasan, R. / Wedekind, J.E. |
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Methods | X-ray diffraction |
Resolution | 1.71 - 3.1 Å |
Structure data | ![]() PDB-6xh0: ![]() PDB-6xh1: ![]() PDB-6xh2: ![]() PDB-6xh3: |
Chemicals | ![]() ChemComp-MG: ![]() ChemComp-HOH: |
Source |
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![]() | RNA 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 |