Specificity of ribonucleoprotein interaction determined by RNA folding during complex formation

The NMR structure of the RNA complex between the regulatory element of the U1A 3'-untranslated region and the U1A protein RNA-binding domain are discussed in a study. Specific intermolecular recognition requires the interaction of the variable loops of the ribonucleoprotein domain with the well...

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Veröffentlicht in:	Nature (London) 1996-04, Vol.380 (6575), p.646-650
Hauptverfasser:	Allain, Frédéric H.-T, Gubser, Charles C, Howe, Peter W. A, Nagai, Kiyoshi, Neuhaus, David, Varani, Gabriele
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Biological and medical sciences Fundamental and applied biological sciences. Psychology Molecular and cellular biology Molecular genetics Molecules NMR Nuclear magnetic resonance Nucleic acids Proteins Ribonucleic acid RNA Rna, ribonucleoproteins Transcription. Transcription factor. Splicing. Rna processing
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Zusammenfassung:	The NMR structure of the RNA complex between the regulatory element of the U1A 3'-untranslated region and the U1A protein RNA-binding domain are discussed in a study. Specific intermolecular recognition requires the interaction of the variable loops of the ribonucleoprotein domain with the well-structured helical regions of the RNA.
ISSN:	0028-0836 1476-4687
DOI:	10.1038/380646a0