The Effect of Mutations on Protein-Protein and Protein-Ligand Interactions for a 17 beta-Hydroxysteroid Dehydrogenase

17beta-hydroxysteroid dehydrogenase type 10, also known as 3-hydroxyacyl CoA dehydrogenase type 2, is variously abbreviated as HSD10, ABAD, ERAB, SDR5C1 or HADH2. The gene for this homotetrameric mitochondrial enzyme, designated as HSD17B10, is found on the X chromosome. Mutations in this protein are associated with neurodegenerative disorders. In addition to its enzymatic activities, HSD10 is a structural component of human ribonuclease P (7ONU.pdb) and is bound to beta-amyloid during Alzheimer's disease (1SO8.pdb). This study examines single nucleotide polymorphisms found in HSD17B10 for their possible effects on protein structure, protein-protein interactions, and protein-ligand interactions, concentrating on the NAD+ binding site. This study compares the mutations that result from these polymorphisms to the sequence differences between rat and human HSD10. References: Kissinger et al, JMB, 342, 943 (2004); Powell et al. JMB 303, 311 (2000); Yang et al. J. Steroid Biochem. Mol. Biol. 143, 460 (2013).