View source for 4uqt


==RRM-peptide structure in RES complex==
<StructureSection load='4uqt' size='340' side='right'caption='[[4uqt]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4uqt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UQT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UQT FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4uqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uqt OCA], [https://pdbe.org/4uqt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uqt RCSB], [https://www.ebi.ac.uk/pdbsum/4uqt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uqt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/IST3_YEAST 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.<ref>PMID:11287609</ref> <ref>PMID:15565172</ref> <ref>PMID:14973223</ref> 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:25160624</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4uqt" style="background-color:#fffaf0;"></div>

==See Also==
*[[Increased sodium tolerance protein|Increased sodium tolerance protein]]
*[[Pre-mRNA splicing factors 3D structures|Pre-mRNA splicing factors 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Barrandon C]]
[[Category: Friberg A]]
[[Category: Sattler M]]
[[Category: Seraphin B]]
[[Category: Tripsianes K]]