Abstract of the PDB Structure's related Publication:
Mitochondrial dysfunction is a hallmark of beta-amyloid (Abeta)-induced neuronal toxicity in Alzheimer's disease (AD). Here, we demonstrate that Abeta-binding alcohol dehydrogenase (ABAD) is a direct molecular link from Abeta to mitochondrial toxicity. Abeta interacts with ABAD in the mitochondria of AD patients and transgenic mice. The crystal structure of Abeta-bound ABAD shows substantial deformation of the active site that prevents nicotinamide adenine dinucleotide (NAD) binding. An ABAD peptide specifically inhibits ABAD-Abeta interaction and suppresses Abeta-induced apoptosis and free-radical generation in neurons. Transgenic mice overexpressing ABAD in an Abeta-rich environment manifest exaggerated neuronal oxidative stress and impaired memory. These data suggest that the ABAD-Abeta interaction may be a therapeutic target in AD.
Part of mitochondrial RNase P which consists of three proteins: MRPP1/TRMT10C, MRPP2/HSD17B10 and MRPP3/KIAA0391. All three are required for the enzyme endonuclease activity while two (MRPP1/TRMT10C, MRPP2/HSD17B10) are sufficient for methyltransferase activity (for more information see the entry for MRPP1/TRMT10C which is the catalytic compound in this complex).