1D3B

CRYSTAL STRUCTURE OF THE D3B SUBCOMPLEX OF THE HUMAN CORE SNRNP DOMAIN AT 2.0A RESOLUTION

Summary for 1D3B

• Entry DOI: 10.2210/pdb1d3b/pdb
• Descriptor: PROTEIN (SMALL NUCLEAR RIBONUCLEOPROTEIN SM D3), PROTEIN (SMALL NUCLEAR RIBONUCLEOPROTEIN ASSOCIATED PROTEIN B), GLYCEROL, ... (5 entities in total)
• Functional Keywords: snrnp, splicing, sm, core snrnp domain, systemic lupus erythematosus, sle, rna binding protein
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm, cytosol : P62318 P14678
• Total number of polymer chains: 12
• Total formula weight: 115644.71

Authors

Kambach, C.,Walke, S.,Avis, J.M.,De La Fortelle, E.,Li, J.,Nagai, K. (deposition date: 1998-12-22, release date: 1999-12-22, 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

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

Experimental method

X-RAY DIFFRACTION (2 Å)