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1B34

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

Summary for 1B34
Entry DOI10.2210/pdb1b34/pdb
DescriptorPROTEIN (SMALL NUCLEAR RIBONUCLEOPROTEIN SM D1), PROTEIN (SMALL NUCLEAR RIBONUCLEOPROTEIN SM D2) (3 entities in total)
Functional Keywordssnrnp, splicing, spliceosome, sm, core snrnp domain, systemic lupus erythematosus, sle, rna binding protein
Biological sourceHomo sapiens (human)
More
Cellular locationNucleus: P62314 P62316
Total number of polymer chains2
Total formula weight26862.58
Authors
Walke, S.,Young, R.J.,Kambach, C.,Avis, J.M.,De La Fortelle, E.,Li, J.,Nagai, K. (deposition date: 1998-12-17, release date: 2000-01-13, Last modification date: 2023-12-27)
Primary citationKambach, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

229183

數據於2024-12-18公開中

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