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TitleStructure of HIV TAR in complex with a Lab-Evolved RRM provides insight into duplex RNA recognition and synthesis of a constrained peptide that impairs transcription.
Journal, issue, pagesNucleic Acids Res., Vol. 46, Page 6401-6415, Year 2018
Publish dateMar 5, 2018 (structure data deposition date)
AuthorsBelashov, I.A. / Crawford, D.W. / Cavender, C.E. / Dai, P. / Beardslee, P.C. / Mathews, D.H. / Pentelute, B.L. / McNaughton, B.R. / Wedekind, J.E.
External linksNucleic Acids Res. / PubMed:29961805
MethodsX-ray diffraction
Resolution1.796 Å
Structure data

PDB-6cmn:
Co-Crystal Structure of HIV-1 TAR Bound to Lab-Evolved RRM TBP6.7
Method: X-RAY DIFFRACTION / Resolution: 1.796 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • oryctolagus cuniculus (rabbit)
  • 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

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