(499.4) The Effect of Mutations on Protein-Protein and Protein-Ligand Interactions for a 17β-Hydroxysteroid Dehydrogenase

Poster Board Number: A206

David Roman (Lehman College, City University of New York), Mary Boldyrev (Pelham Memorial High School), Song-Yu Yang (The Graduate Center City University of New York CUNY, The Graduate Center City University of New York CUNY), Manfred Philipp (The Graduate Center City University of New York CUNY)

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 Alzheimers 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)



Differences Between Rat and Human HSD10 Projected on the Monomeric Human 1U7T Structure