4oz1: Difference between revisions
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''' | ==Crystal structure of human CAPERalpha UHM bound to SF3b155 ULM5== | ||
<StructureSection load='4oz1' size='340' side='right' caption='[[4oz1]], [[Resolution|resolution]] 1.74Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4oz1]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OZ1 OCA]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=LYS:LYSINE'>LYS</scene><br> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4oz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oz1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oz1 RCSB], [http://www.ebi.ac.uk/pdbsum/4oz1 PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
U2AF Homology Motifs (UHMs) mediate protein-protein interactions with U2AF Ligand Motifs (ULMs) of pre-mRNA splicing factors. The UHM-containing alternative splicing factor CAPERalpha regulates splicing of tumor-promoting VEGF isoforms, yet the molecular target of the CAPERalpha UHM is unknown. Here, we present structures of the CAPERalpha UHM bound to a representative SF3b155 ULM at 1.7 A resolution, and for comparison, in the absence of ligand at 2.2 A resolution. The prototypical UHM/ULM interactions authenticate CAPERalpha as a bona fide member of the UHM-family of proteins. We identify SF3b155 as the relevant ULM-containing partner of full-length CAPERalpha in human cell extracts. Isothermal titration calorimetry comparisons of the purified CAPERalpha UHM binding known ULM-containing proteins demonstrate that high affinity interactions depend on the presence of an intact, intrinsically-unstructured SF3b155 domain containing seven ULM-like motifs. The interplay among bound CAPERalpha molecules gives rise to the appearance of two high affinity sites in the SF3b155 ULM-containing domain. In conjunction with the previously-identified, UHM/ULM-mediated complexes of U2AF65 and SPF45 with SF3b155, this work demonstrates the capacity of SF3b155 to offer a platform for coordinated recruitment of UHM-containing splicing factors. | |||
Cancer-Relevant Splicing Factor CAPERalpha Engages the Essential Splicing Factor SF3b155 in a Specific Ternary Complex.,Loerch S, Maucuer A, Manceau V, Green MR, Kielkopf CL J Biol Chem. 2014 May 2. PMID:24795046<ref>PMID:24795046</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Kielkopf, C L.]] | |||
[[Category: Loerch, S.]] | |||
[[Category: Pre-mrna splicing factor]] | |||
[[Category: Protein-peptide complex]] | |||
[[Category: U2af homology motif]] | |||
[[Category: Uhm]] | |||
