Crystal Structures of Two Sm Protein Complexes and Their Implications for the Assembly of the Spliceosomal snRNPs
| Autor: | Veronica A. Raker, Johanna M. Avis, Reinhard Lührmann, C. Kambach, Robert I. M. Young, Kiyoshi Nagai, Jade Li, Eric de La Fortelle, S. Walke |
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| Rok vydání: | 1999 |
| Předmět: |
Models
Molecular Protein Folding Macromolecular Substances RNA Splicing Molecular Sequence Data Beta sheet RNA-binding protein Biology Antiparallel (biochemistry) Crystallography X-Ray Autoantigens General Biochemistry Genetics and Molecular Biology Protein structure RNA Small Nuclear snRNP Amino Acid Sequence Conserved Sequence SnRNP Biogenesis Biochemistry Genetics and Molecular Biology(all) Ribonucleoproteins Small Nuclear Molecular biology Peptide Fragments Protein Structure Tertiary Crystallography Spliceosomes Sequence motif Dimerization Small nuclear ribonucleoprotein |
| Zdroj: | Cell. 96(3):375-387 |
| ISSN: | 0092-8674 |
| DOI: | 10.1016/s0092-8674(00)80550-4 |
| Popis: | The U1, U2, U4/U6, and U5 small nuclear ribonucleoprotein particles (snRNPs) involved in pre-mRNA splicing contain seven Sm proteins (B/B′, D1, D2, D3, E, F, and G) in common, which assemble around the Sm site present in four of the major spliceosomal small nuclear RNAs (snRNAs). These proteins share a common sequence motif in two segments, Sm1 and Sm2, separated by a short variable linker. Crystal structures of two Sm protein complexes, D3B and D1D2, show that these proteins have a common fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel β sheet, and the D1D2 and D3B dimers superpose closely in their core regions, including the dimer interfaces. The crystal structures suggest that the seven Sm proteins could form a closed ring and the snRNAs may be bound in the positively charged central hole. |
| Databáze: | OpenAIRE |
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