1B34
CRYSTAL STRUCTURE OF THE D1D2 SUB-COMPLEX FROM THE HUMAN SNRNP CORE DOMAIN
Summary for 1B34
Entry DOI | 10.2210/pdb1b34/pdb |
Descriptor | PROTEIN (SMALL NUCLEAR RIBONUCLEOPROTEIN SM D1), PROTEIN (SMALL NUCLEAR RIBONUCLEOPROTEIN SM D2) (3 entities in total) |
Functional Keywords | snrnp, splicing, spliceosome, sm, core snrnp domain, systemic lupus erythematosus, sle, rna binding protein |
Biological source | Homo sapiens (human) More |
Cellular location | Nucleus: P62314 P62316 |
Total number of polymer chains | 2 |
Total formula weight | 26862.58 |
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 citation | 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 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: 10025403DOI: 10.1016/S0092-8674(00)80550-4 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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