Crystal structure at 1.92 Å resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin
doi: 10.1038/372432a0
pmid: 7984237
Crystal structure at 1.92 Å resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin
The crystal structure of the RNA-binding domain of the small nuclear ribonucleoprotein U1A bound to a 21-nucleotide RNA hairpin has been determined at 1.92 A resolution. The ten-nucleotide RNA loop binds to the surface of the beta-sheet as an open structure, and the AUUGCAC sequence of the loop interacts extensively with the conserved RNP1 and RNP2 motifs and the C-terminal extension of the RNP domain. These interactions include stacking of RNA bases with aromatic side chains of proteins and many direct and water-mediated hydrogen bonds. The structure reveals the stereochemical basis for sequence-specific RNA recognition by the RNP domain.
- European Molecular Biology Laboratory Germany
- Medical Research Council United Kingdom
- European Bioinformatics Institute United Kingdom
- University of Leeds United Kingdom
- MRC Laboratory of Molecular Biology United Kingdom
Models, Molecular, Binding Sites, Base Sequence, Molecular Sequence Data, RNA-Binding Proteins, Hydrogen Bonding, Crystallography, X-Ray, Protein Structure, Secondary, Protein Structure, Tertiary, Ribonucleoprotein, U1 Small Nuclear, RNA, Small Nuclear, Spliceosomes, Nucleic Acid Conformation, Amino Acid Sequence
Models, Molecular, Binding Sites, Base Sequence, Molecular Sequence Data, RNA-Binding Proteins, Hydrogen Bonding, Crystallography, X-Ray, Protein Structure, Secondary, Protein Structure, Tertiary, Ribonucleoprotein, U1 Small Nuclear, RNA, Small Nuclear, Spliceosomes, Nucleic Acid Conformation, Amino Acid Sequence
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