6tyt

Structure of Ku80 von Willebrand domain S229A mutant complexed with APLF and XLF Ku Binding Motif

spinqualitylabelsall models 6tyt, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6tyt is a 3 chain structure with sequence from Homo sapiens and Xenopus laevis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.403488Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1L8ENT6_XENLA 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ku protein

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