eless , ▁V D AC 3 ▁demonstr ates ▁limited ▁p ore - form ing ▁ability ▁and , ▁instead , ▁interact s ▁with ▁other ▁prote ins ▁to ▁perform ▁its ▁bi ological ▁functions , ▁including ▁s perm ▁flag ella ▁assembly ▁and ▁cent ri ole ▁assembly . ▁Mut ations ▁in ▁V D AC 3 ▁have ▁been ▁linked ▁to ▁male ▁infer til ity , ▁as ▁well ▁as ▁Park inson ’ s ▁disease . ▁ ▁Str ucture ▁ ▁The ▁three ▁V D AC ▁is o forms ▁in ▁human ▁are ▁highly ▁conser ved , ▁particularly ▁with ▁respect ▁to ▁their ▁ 3 D ▁structure . ▁V D AC s ▁form ▁a ▁wide ▁ β - bar rel ▁structure , ▁inside ▁of ▁which ▁the ▁N - term inal ▁res ides ▁to ▁partially ▁close ▁the ▁p ore . ▁The ▁sequence ▁of ▁the ▁V D AC 3 ▁is o form ▁contains ▁an ▁abund ance ▁of ▁c yst e ines , ▁which ▁allow ▁for ▁the ▁formation ▁of ▁dis ulf ide ▁brid ges ▁and , ▁ultimately , ▁affect ▁the ▁flex ibility ▁of ▁the ▁ β - bar rel . ▁V D AC s ▁also ▁contain ▁a ▁mit och ond rial ▁target ing ▁sequence ▁for ▁the ▁protein ' s ▁trans location ▁to ▁the ▁outer ▁mit och ond rial ▁memb rane . ▁V D AC 3 ▁still ▁yet ▁poss esses ▁multiple ▁is o forms , ▁including ▁a ▁full - length ▁form ▁and ▁shorter ▁form ▁term ed ▁V D AC 3 b . ▁This ▁shorter ▁form ▁is ▁pre domin antly ▁expressed ▁over ▁the ▁full - length ▁form ▁at