The Structure of the Stemloop D Subdomain of Coxsackievirus B3 Cloverleaf RNA and Its Interaction with the Proteinase 3C(623 views) Ohlenschlager O, Wohnert J, Bucci E, Seitz S, Hafner S, Ramachandran R, Zell R, Gorlach M
Inst. F. Molec. Biotechnologie e.V., Bentenbergstr. 100813, D-07745 Jena, Germany
Ist. di Biostrutture e Bioimmagini, Via Mezzocannone 6-8, I-80134 Napoli, Italy
Inst. F. Virologie Antivirale T., Friedrich-Schiller-Universität, Winzerlaer Straße 10, D-07745 Jena, Germany
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Theimer, C. A., Finger, L. D., Trantirek, L., Feigon, J., Mutations linked to dyskeratosis congenita cause changes in the structural equilibrium in telomerase RNA (2003) Proc. Natl. Acad. Sci. USA, 100, pp. 449-454
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W hnert, J., Dingley, A. J., Stoldt, M., G rlach, M., Grzesiek, S., Brown, L. R., Direct identification of NH N hydrogen bonds in non-canonical base pairs of RNA by NMR spectroscopy (1999) Nucleic Acids Res., 27, pp. 3104-3110
W hnert, J., G rlach, M., Schwalbe, H., Triple resonance experiments for the simultaneous correlation of H5/H6 and exchangeable hydrogens of pyrimidine nucleotides in 13C, 15N-labeled RNA applicable to larger RNA molecules (2003) J. Biomol. NMR, 26, pp. 79-83
The Structure of the Stemloop D Subdomain of Coxsackievirus B3 Cloverleaf RNA and Its Interaction with the Proteinase 3C
Stemloop D (SLD) of the 5′ cloverleaf RNA is the cognate ligand of the coxsackievirus B3 (CVB3) 3C proteinase (3Cpro). Both are indispensable components of the viral replication initiation complex. SLD is a structurally autonomous subunit of the 5′ cloverleaf. The SLD structure was solved by NMR spectroscopy to an rms deviation of 0.66 Å (all heavy atoms). SLD contains a novel triple pyrimidine mismatch motif with a central Watson-Crick type C:U pair. SLD is capped by an apical uCACGg tetraloop adopting a structure highly similar to stable cUNCGg tetraloops. Binding of CVB3 3Cpro induces changes in NMR spectra for nucleotides adjacent to the triple pyrimidine mismatch and of the tetraloop implying them as sites of specific SLD:3Cpro interaction. The binding of 3Cpro to SLD requires the integrity of those structural elements, strongly suggesting that 3Cpro recognizes a structural motif instead of a specific sequence.
The Structure of the Stemloop D Subdomain of Coxsackievirus B3 Cloverleaf RNA and Its Interaction with the Proteinase 3C
No results.
The Structure of the Stemloop D Subdomain of Coxsackievirus B3 Cloverleaf RNA and Its Interaction with the Proteinase 3C
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