4uqt | pdb_00004uqt

RRM-peptide structure in RES complex

spinqualitylabelsall models 4uqt, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4uqt is a 2 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, RCSB, PDBsum Function [IST3_YEAST] Required for pre-mRNA splicing and spliceosome assembly. As part of the pre-mRNA retention and splicing (RES) complex, required for nuclear pre-mRNA retention and efficient splicing. Required for MER1-activated splicing. [CWC26_YEAST] Required for efficient splicing and pre-mRNA nuclear retention. May also be involved in positioning the proximal bud pole signal. Publication Abstract from PubMed The REtention and Splicing (RES) complex is a conserved spliceosome-associated module that was shown to enhance splicing of a subset of transcripts and to promote the nuclear retention of unspliced pre-mRNAs in yeast. The heterotrimeric RES complex is organized around the Snu17p protein that binds to both the Bud13p and Pml1p subunits. Snu17p exhibits an RRM domain that resembles a U2AF homology motif (UHM) and Bud13p harbors a Trp residue reminiscent of an UHM-ligand motif (ULM). It has therefore been proposed that the interaction between Snu17p and Bud13p resembles canonical UHM-ULM complexes. Here, we have used biochemical and NMR structural analysis to characterize the structure of the yeast Snu17p-Bud13p complex. Unlike known UHMs that sequester the Trp residue of the ULM ligand in a hydrophobic pocket, Snu17p and Bud13p utilize a large interaction surface formed around the two helices of the Snu17p domain. In total eighteen residues of Bud13p ligand wrap around the Snu17p helical surface in an U-turn-like arrangement. The invariant Trp232 in Bud13p is located in the center of the turn, and contacts surface residues of Snu17p. The structural data are supported by mutational analysis and indicate that the Snu17p provides an extended binding surface with Bud13p that is notably distinct from canonical UHM-ULM interactions. Our data highlight structural diversity in RNA recognition motif (RRM)-protein interactions, analogous to the one seen in for nucleic acid interactions. A Novel Protein-Protein Interaction in the RES (REtention and Splicing) Complex.,Tripsianes K, Friberg A, Barrandon C, Brooks M, van Tilbeurgh H, Seraphin B, Sattler M J Biol Chem. 2014 Aug 26. pii: jbc.M114.592311. PMID:25160624 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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