3PGW

Crystal structure of human U1 snRNP

Summary for 3PGW

• Entry DOI: 10.2210/pdb3pgw/pdb
• Descriptor: U1-A, U1 snRNA, DNA 5'-D(*AP*GP*GP*TP*AP*AP*GP*TP*A)-3', ... (11 entities in total)
• Functional Keywords: protein-rna complex, u1 snrna, sm fold, sm core, rrm, splicing, mrna, snrnps, splicing factors, splicing-dna-rna complex, splicing/dna/rna
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: P09012 P08621 Q66K91; Cytoplasm, cytosol : P62318 P62314 P62316 P62306 P62304
• Total number of polymer chains: 22
• Total formula weight: 464104.82

Authors

Weber, G.,Trowitzsch, S.,Kastner, B.,Luehrmann, R.,Wahl, M.C. (deposition date: 2010-11-02, release date: 2010-12-29, Last modification date: 2024-02-21)

Primary citation

Weber, G.,Trowitzsch, S.,Kastner, B.,Luhrmann, R.,Wahl, M.C.
Functional organization of the Sm core in the crystal structure of human U1 snRNP.
Embo J., 29:4172-4184, 2010

PubMed Abstract: U1 small nuclear ribonucleoprotein (snRNP) recognizes the 5'-splice site early during spliceosome assembly. It represents a prototype spliceosomal subunit containing a paradigmatic Sm core RNP. The crystal structure of human U1 snRNP obtained from natively purified material by in situ limited proteolysis at 4.4 Å resolution reveals how the seven Sm proteins, each recognize one nucleotide of the Sm site RNA using their Sm1 and Sm2 motifs. Proteins D1 and D2 guide the snRNA into and out of the Sm ring, and proteins F and E mediate a direct interaction between the Sm site termini. Terminal extensions of proteins D1, D2 and B/B', and extended internal loops in D2 and B/B' support a four-way RNA junction and a 3'-terminal stem-loop on opposite sides of the Sm core RNP, respectively. On a higher organizational level, the core RNP presents multiple attachment sites for the U1-specific 70K protein. The intricate, multi-layered interplay of proteins and RNA rationalizes the hierarchical assembly of U snRNPs in vitro and in vivo.

PubMed: 21113136
DOI: 10.1038/emboj.2010.295

Experimental method

X-RAY DIFFRACTION (4.4 Å)