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

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 leu...

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Bibliographic Details
Published in:Nature (London) 1998-08, Vol.394 (6694), p.645-650
Main Authors: Price, Stephen R., Evans, Philip R., Nagai, Kiyoshi
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Autoantigens
Biological and medical sciences
Crystalline structure
Crystallography, X-Ray
Crystals
Drosophila
Drosophila Proteins
Evolution, Molecular
Fundamental and applied biological sciences. Psychology
Humanities and Social Sciences
Humans
Models, Molecular
Molecular biology
Molecular biophysics
Molecular Sequence Data
multidisciplinary
Nucleic Acid Conformation
Protein Binding
Protein Conformation
Proteins
Proteins - chemistry
Recombinant Proteins - chemistry
Ribonucleic acid
Ribonucleoprotein, U1 Small Nuclear - chemistry
Ribonucleoprotein, U2 Small Nuclear - chemistry
Ribonucleoprotein, U2 Small Nuclear - metabolism
Ribonucleoproteins, Small Nuclear
RNA
RNA, Small Nuclear - chemistry
RNA, Small Nuclear - metabolism
RNA-Binding Proteins
Science
Science (multidisciplinary)
snRNP Core Proteins
Structure in molecular biology
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Summary: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.
ISSN:0028-0836
1476-4687
DOI:10.1038/29234