Literature DB >> 12176065

Recognition of diverse RNAs by a single protein structural framework.

Marc Spingola1, Francis Lim, David S Peabody.   

Abstract

The coat proteins of different single-strand RNA phages utilize a common structural framework to recognize different RNA targets, making them suitable models for studies of RNA-protein recognition generally, especially for the class of proteins that bind RNA on a beta-sheet surface. Here we show that structurally distinct molecules are capable of satisfying the requirements for binding to Qbeta coat protein. Although the predicted secondary structures of the RNAs differ markedly, we contend that they are approximately equivalent structurally in their complexes with coat protein. Based on our prior observations that the RNA-binding specificities of Qbeta and MS2 coat proteins can be interconverted with as few as one amino acid substitution each, and taking into account details of the structures of complexes of MS2 coat protein with wild-type and aptamer RNAs, we propose a model for the Qbeta coat protein-RNA complex.

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Year:  2002        PMID: 12176065     DOI: 10.1016/s0003-9861(02)00334-x

Source DB:  PubMed          Journal:  Arch Biochem Biophys        ISSN: 0003-9861            Impact factor:   4.013


  3 in total

1.  RNA recognition site of PP7 coat protein.

Authors:  Francis Lim; David S Peabody
Journal:  Nucleic Acids Res       Date:  2002-10-01       Impact factor: 16.971

2.  High-affinity binding site for a group II intron-encoded reverse transcriptase/maturase within a stem-loop structure in the intron RNA.

Authors:  Kazuo Watanabe; Alan M Lambowitz
Journal:  RNA       Date:  2004-07-23       Impact factor: 4.942

3.  Structural basis of RNA binding discrimination between bacteriophages Qbeta and MS2.

Authors:  Wilf T Horn; Kaspars Tars; Elin Grahn; Charlotte Helgstrand; Andrew J Baron; Hugo Lago; Chris J Adams; David S Peabody; Simon E V Phillips; Nicola J Stonehouse; Lars Liljas; Peter G Stockley
Journal:  Structure       Date:  2006-03       Impact factor: 5.006

  3 in total

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