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Title
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Crystal structure at 1.92 A resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin.
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Authors
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C.Oubridge,
N.Ito,
P.R.Evans,
C.H.Teo,
K.Nagai.
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Ref.
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Nature, 1994,
372,
432-438.
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PubMed id
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Abstract
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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.
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