View source for 2m09


==Structure, phosphorylation and U2AF65 binding of the Nterminal Domain of splicing factor 1 during 3 splice site Recognition==
<StructureSection load='2m09' size='340' side='right'caption='[[2m09]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2m09]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M09 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M09 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=2m09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m09 OCA], [https://pdbe.org/2m09 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m09 RCSB], [https://www.ebi.ac.uk/pdbsum/2m09 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m09 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SF01_HUMAN SF01_HUMAN] Necessary for the ATP-dependent first step of spliceosome assembly. Binds to the intron branch point sequence (BPS) 5'-UACUAAC-3' of the pre-mRNA. May act as transcription repressor.<ref>PMID:8752089</ref> <ref>PMID:10449420</ref> <ref>PMID:9660765</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Recognition of the 3'-splice site is a key step in pre-mRNA splicing and accomplished by a dynamic complex comprising splicing factor 1 (SF1) and the U2 snRNP auxiliary factor 65-kDa subunit (U2AF65). Both proteins mediate protein-protein and protein-RNA interactions for cooperative RNA-binding during spliceosome assembly. Here, we report the solution structure of a novel helix-hairpin domain in the N-terminal region of SF1 (SF1(NTD)). The nuclear magnetic resonance- and small-angle X-ray scattering-derived structure of a complex of the SF1(NTD) with the C-terminal U2AF homology motif domain of U2AF65 (U2AF65(UHM)) reveals that, in addition to the known U2AF65(UHM)-SF1 interaction, the helix-hairpin domain forms a secondary, hydrophobic interface with U2AF65(UHM), which locks the orientation of the two subunits. Mutational analysis shows that the helix hairpin is essential for cooperative formation of the ternary SF1-U2AF65-RNA complex. We further show that tandem serine phosphorylation of a conserved Ser80-Pro81-Ser82-Pro83 motif rigidifies a long unstructured linker in the SF1 helix hairpin. Phosphorylation does not significantly alter the overall conformations of SF1, SF1-U2AF65 or the SF1-U2AF65-RNA complexes, but slightly enhances RNA binding. Our results indicate that the helix-hairpin domain of SF1 is required for cooperative 3'-splice site recognition presumably by stabilizing a unique quaternary arrangement of the SF1-U2AF65-RNA complex.

Structure, phosphorylation and U2AF65 binding of the N-terminal domain of splicing factor 1 during 3'-splice site recognition.,Zhang Y, Madl T, Bagdiul I, Kern T, Kang HS, Zou P, Mausbacher N, Sieber SA, Kramer A, Sattler M Nucleic Acids Res. 2013 Jan 1;41(2):1343-1354. Epub 2012 Nov 21. PMID:23175611<ref>PMID:23175611</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2m09" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Bagdiul I]]
[[Category: Kang H]]
[[Category: Kern T]]
[[Category: Kraemer A]]
[[Category: Madl T]]
[[Category: Maeusbacher N]]
[[Category: Sattler M]]
[[Category: Sieber SA]]
[[Category: Zhang Y]]
[[Category: Zou P]]