▁N - ter minus ▁of ▁T CF ▁adapted ▁what ▁appeared ▁to ▁be ▁a ▁rig id ▁con formation , ▁with ▁the ▁binding ▁mot if ▁sp anning ▁many ▁beta - c aten in ▁repe ats . ▁ ▁Rel atively ▁strong ▁charged ▁interaction ▁" hot ▁sp ots " ▁were ▁defined ▁( pred icted , ▁and ▁later ▁verified , ▁to ▁be ▁conser ved ▁for ▁the ▁beta - c aten in / E - c ad her in ▁interaction ), ▁as ▁well ▁as ▁hydro ph ob ic ▁regions ▁de emed ▁important ▁in ▁the ▁overall ▁mode ▁of ▁binding ▁and ▁as ▁potential ▁th era pe ut ic ▁small ▁mole c ule ▁in hib itor ▁targets ▁against ▁certain ▁cancer ▁forms . ▁ ▁Furthermore , ▁following ▁studies ▁demonstrated ▁another ▁peculiar ▁characteristic , ▁pl astic ity ▁in ▁the ▁binding ▁of ▁the ▁T CF ▁N - ter minus ▁to ▁beta - c aten in . ▁ ▁Similarly , ▁we ▁find ▁the ▁familiar ▁E - c ad her in , ▁whose ▁cy top las m atic ▁tail ▁contacts ▁the ▁AR M ▁domain ▁in ▁the ▁same ▁canonical ▁fashion . ▁The ▁sc aff old ▁protein ▁ax in ▁( two ▁closely ▁related ▁par al ogs , ▁ax in ▁ 1 ▁and ▁ax in ▁ 2 ) ▁contains ▁a ▁similar ▁interaction ▁mot if ▁on ▁its ▁long , ▁dis ordered ▁middle ▁segment . ▁Although ▁one ▁mole c ule ▁of ▁ax in ▁only ▁contains ▁a ▁single ▁ β - c aten in ▁rec ruit ment ▁mot if , ▁its ▁partner ▁the ▁A den om at ous ▁Poly pos is ▁Col i