Crystal structure at 1.92 Å resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1994-12

AUTHORS

C Oubridge, N Ito, P R Evans, C H Teo, K Nagai

ABSTRACT

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. More... »

PAGES

432-438

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/372432a0

DOI

http://dx.doi.org/10.1038/372432a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1036365135

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/7984237


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