IndraLab

Statements

BRCC3 binds Abraxas. 4 / 4
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"However, since both Abraxas and Abro1 each bind to both BRCC36 and BRCC45 in their respective DUB complexes, we surmised that the interaction surfaces for these components should show the highest degree of conservation between the two paralogs."
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"Abraxas and Brcc36 associate through coiled-coil domains on each protein."
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"The structure of an active core complex comprising twoAbraxas/BRCC36/BRCC45/MERIT40 tetramers determined by negative-stain electron microscopy (EM) reveals a distorted V-shape architecture in which a dimer of Abraxas and BRCC36 heterodimers sits at the base, with BRCC45 and Merit40 pairs occupying each arm."
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"Thus, it seems likely that the apparent requirement of BRCC45 for DUB activity of the BRCA1-A complex, but not BRISC, is not due to major structural differences between the two complexes, but merely reflects a specific stabilizing effect of BRCC45 on Abraxas and BRCC36 complexes that is not required by Abro1 and BRCC36."
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