Crystal structure of the spliceosomal U2B″–U2A′ protein complex bound to a fragment of U2 small nuclear RNA

Stephen R. Price, Philip R. Evans and Kiyoshi Nagai ()
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Stephen R. Price: Columbia University
Philip R. Evans: MRC Laboratory of Molecular Biology
Kiyoshi Nagai: MRC Laboratory of Molecular Biology

Nature, 1998, vol. 394, issue 6694, 645-650

Abstract: Abstract We have determined the crystal structure at 2.4 å resolution of a ternary complex between the spliceosomal U2B″/U2A′ protein complex and hairpin-loop IV of U2 small nuclear RNA. Unlike its close homologue the U1A protein, U2B″ binds to its cognate RNA only in the presence of U2A′, which contains leucine-rich repeats in its sequence. The concave surface of a parallel β-sheet within the leucine-rich-repeat region of U2A′ interacts with the ribonucleoprotein domain of U2B″ on the surface opposite its RNA-binding surface. The basic carboxy-terminal region of U2A′ interacts with the RNA stem. The crystal structure reveals how protein–protein interaction regulates RNA-binding specificity, and how replacing only a few key residues allows the U2B″ and U1A proteins to discriminate between their cognate RNA hairpins by forming alternative networks of interactions.

Date: 1998
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DOI: 10.1038/29234

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