The eukaryotic Sm and Sm-like (Lsm) proteins associate with RNA to form the core domain of the ribonucleoprotein particles involved in a variety of RNA processing events including pre-mRNA splicing, telomere replication, and mRNA degradation. Members of this family share a highly conserved Sm fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel β-sheet [, , ]. Lsm11 is an SmD2-like subunit which binds U7 snRNA along with Lsm10 and five other Sm subunits to form a 7-membered ring structure. Lsm11 and the U7 snRNP of which it is a part are thought to play an important role in histone mRNA 3' processing [, ].
This entry represents the middle domain of Lsm11.The eukaryotic Sm and Sm-like (Lsm) proteins associate with RNA to form the core domain of the ribonucleoprotein particles involved in a variety of RNA processing events including pre-mRNA splicing, telomere replication, and mRNA degradation. Members of this family share a highly conserved Sm fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel β-sheet [, , ]. Lsm11 is an SmD2-like subunit which binds U7 snRNA along with Lsm10 and five other Sm subunits to form a 7-membered ring structure. Lsm11 and the U7 snRNP of which it is a part are thought to play an important role in histone mRNA 3' processing [, ].
