Tudor domain found in survival motor neuron protein (SMN) and similar proteins
SMN, also called component of gems 1, or Gemin-1, is part of a multimeric SMN complex that includes spliceosomal Sm core proteins and plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Mutations in human SMN lead to motor neuron degeneration and spinal muscular atrophy. SMN contains a central, highly conserved Tudor domain that is required for U snRNP assembly and Sm protein binding and has been shown to bind arginine-glycine-rich motifs in an methylarginine-dependent manner.
Feature 1:peptide binding site [polypeptide binding site]
Evidence:
Comment:In general, the Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.
Structure:4A4E; Homo sapiens SMN Tudor domain in complex with symmetrically dimethylated arginine at the peptide ligand binding site, contacts at 4A - View structure with Cn3D
Structure:4QQ6; Homo sapiens SMN Tudor domain in complex with a small organic molecule (4-Methyl-2,3,4,5,6,7-Hexahydrodicyclopenta[b,E]pyridin-8(1h)-Imine), contacts at 4A - View structure with Cn3D
Jiyao W et al.(2023). "The conserved domain database in 2023.",