View source for 6tyx


==Structure of Ku80 von Willebrand domain S229A mutant complexed with XLF Ku Binding Motif==
<StructureSection load='6tyx' size='340' side='right'caption='[[6tyx]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6tyx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TYX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TYX FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8994435&#8491;</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=6tyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tyx OCA], [https://pdbe.org/6tyx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tyx RCSB], [https://www.ebi.ac.uk/pdbsum/6tyx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tyx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1L8ENT6_XENLA A0A1L8ENT6_XENLA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The N-terminal von Willebrand domain of Ku80 supports interactions with a Ku binding motif (KBM) that has been identified in at least three other DNA repair proteins: the non-homologous end joining (NHEJ) scaffold APLF, the modulator of retrovirus infection, MRI, and the Werner syndrome protein (WRN). A second, more recently identified Ku binding motif present in XLF and several other proteins (KBMX) has also been reported to interact with this domain. The isolated Ku80 von Willebrand antigen domain (vWA) from Xenopus laevis has a sequence that is 60% identical with the human domain, is readily expressed and has been used to investigate these interactions. Structural characterization of the complexes formed with the KBM motifs in human APLF, MRI, and WRN identify a conserved binding site that is consistent with previously-reported mutational studies. In contrast with the KBM binding site, structural studies indicate that the KBMX site is occluded by a distorted helix. Fluorescence polarization and (19)F NMR studies of a fluorinated XLF C-terminal peptide failed to indicate any interaction with the frog vWA. It was hypothesized that availability of this binding site is conditional, i.e., dependent on specific experimental conditions or other repair factors to make the site available for binding. Modulating the fraction of KBMX-accessible binding site mutationally demonstrated that the more open site is capable of binding the KBMX(XLF) motif peptide. It is suggested that the conditional nature of KBMX binding limits formation of non-productive complexes so that activation-dependent site availability can more optimally support advancing the synapsis process.

Ligand binding characteristics of the Ku80 von Willebrand domain.,Kim K, Min J, Kirby TW, Gabel SA, Pedersen LC, London RE DNA Repair (Amst). 2019 Oct 24;85:102739. doi: 10.1016/j.dnarep.2019.102739. PMID:31733588<ref>PMID:31733588</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6tyx" style="background-color:#fffaf0;"></div>

==See Also==
*[[Ku protein|Ku protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Xenopus laevis]]
[[Category: Min J]]
[[Category: Pedersen LC]]