B 1 0 0 ▁are ▁in ▁an ▁am ph ip ath ic ▁condition , ▁the ▁structure ▁of ▁some ▁of ▁its ▁domains ▁is ▁dependent ▁on ▁underlying ▁li pid ▁conditions . ▁However , ▁it ▁is ▁known ▁to ▁have ▁the ▁same ▁overall ▁fol ding ▁in ▁L DL ▁having ▁five ▁main ▁domains . ▁Rec ently ▁the ▁first ▁structure ▁of ▁L DL ▁at ▁human ▁body ▁temperature ▁in ▁native ▁condition ▁has ▁been ▁found ▁using ▁cry o - elect ron ▁micro sc opy ▁at ▁a ▁resolution ▁of ▁ 1 6 ▁Ang st rom . ▁The ▁overall ▁fol ding ▁of ▁A po B - 1 0 0 ▁has ▁been ▁confirmed ▁and ▁some ▁heter ogene ity ▁in ▁the ▁local ▁structure ▁of ▁its ▁domains ▁have ▁been ▁mapped . ▁ ▁Function ▁ ▁Edit ing ▁is ▁restricted ▁to ▁those ▁trans cript s ▁expressed ▁in ▁the ▁small ▁int est ine . ▁This ▁shorter ▁version ▁of ▁the ▁protein ▁has ▁a ▁function ▁specific ▁to ▁the ▁small ▁int est ine . ▁The ▁main ▁function ▁of ▁the ▁full ▁length ▁li ver ▁expressed ▁A po B 1 0 0 ▁is ▁as ▁a ▁lig and ▁for ▁activation ▁of ▁the ▁L DL - R . ▁However , ▁editing ▁results ▁in ▁a ▁protein ▁lack ing ▁this ▁L DL - R ▁binding ▁region ▁of ▁the ▁protein . ▁This ▁al ters ▁the ▁function ▁of ▁the ▁protein ▁and ▁the ▁shorter ▁A po B 4 8 ▁protein ▁as ▁specific ▁functions ▁relative ▁to ▁the ▁small ▁int est ine . ▁A po B 4 8 ▁is ▁identical ▁to ▁the ▁am ino - term inal ▁ 4 8 % ▁of ▁A