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

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  • Stephen R. Price

    (Columbia University)

  • Philip R. Evans

    (MRC Laboratory of Molecular Biology)

  • Kiyoshi Nagai

    (MRC Laboratory of Molecular Biology)

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.

Suggested Citation

  • Stephen R. Price & Philip R. Evans & Kiyoshi Nagai, 1998. "Crystal structure of the spliceosomal U2B″–U2A′ protein complex bound to a fragment of U2 small nuclear RNA," Nature, Nature, vol. 394(6694), pages 645-650, August.
    • Handle: RePEc:nat:nature:v:394:y:1998:i:6694:d:10.1038_29234
    DOI: 10.1038/29234
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