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The NMR and X-ray structures of the Saccharomyces cerevisiae Vts1 SAM domain define a surface for the recognition of RNA hairpins.
Aviv, Tzvi; Amborski, Andrew N; Zhao, X Sharon; Kwan, Jamie J; Johnson, Philip E; Sicheri, Frank; Donaldson, Logan W.
Afiliação
  • Aviv T; Program in Molecular Biology and Cancer, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ont., Canada.
J Mol Biol ; 356(2): 274-9, 2006 Feb 17.
Article em En | MEDLINE | ID: mdl-16375924
The SAM domain of the Saccharomyces cerevisiae post-transcriptional regulator Vts1 has a high affinity towards RNA hairpins containing a CUGGC pentaloop. We present the 1.6 Angstroms X-ray crystal structure of the Vts1 SAM domain in its unliganded state, and the NMR solution structure of this domain in its RNA-bound state. Both structures reveal a canonical five helix SAM domain flanked by additional secondary structural elements at the N and C termini. The two structures are essentially identical, implying that no major structural rearrangements occur upon RNA binding. Amide chemical shift changes map the RNA-binding site to a shallow, basic patch at the junction of helix alpha5 and the loop connecting helices alpha1 and alpha2.
Assuntos
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Base de dados: MEDLINE Assunto principal: RNA / Proteínas de Ligação a RNA / Estrutura Terciária de Proteína / Proteínas de Saccharomyces cerevisiae / Conformação de Ácido Nucleico Idioma: En Revista: J Mol Biol Ano de publicação: 2006 Tipo de documento: Article País de afiliação: Canadá
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Base de dados: MEDLINE Assunto principal: RNA / Proteínas de Ligação a RNA / Estrutura Terciária de Proteína / Proteínas de Saccharomyces cerevisiae / Conformação de Ácido Nucleico Idioma: En Revista: J Mol Biol Ano de publicação: 2006 Tipo de documento: Article País de afiliação: Canadá