1B34

CRYSTAL STRUCTURE OF THE D1D2 SUB-COMPLEX FROM THE HUMAN SNRNP CORE DOMAIN

1B34 の概要

• エントリーDOI: 10.2210/pdb1b34/pdb
• 分子名称: PROTEIN (SMALL NUCLEAR RIBONUCLEOPROTEIN SM D1), PROTEIN (SMALL NUCLEAR RIBONUCLEOPROTEIN SM D2) (3 entities in total)
• 機能のキーワード: snrnp, splicing, spliceosome, sm, core snrnp domain, systemic lupus erythematosus, sle, rna binding protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: P62314 P62316
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 26862.58

構造登録者

Walke, S.,Young, R.J.,Kambach, C.,Avis, J.M.,De La Fortelle, E.,Li, J.,Nagai, K. (登録日: 1998-12-17, 公開日: 2000-01-13, 最終更新日: 2023-12-27)

主引用文献

Kambach, C.,Walke, S.,Young, R.,Avis, J.M.,de la Fortelle, E.,Raker, V.A.,Luhrmann, R.,Li, J.,Nagai, K.
Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs.
Cell(Cambridge,Mass.), 96:375-387, 1999

PubMed Abstract: 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 beta 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.

PubMed: 10025403
DOI: 10.1016/S0092-8674(00)80550-4

実験手法

X-RAY DIFFRACTION (2.5 Å)