The ATP binding cassette (ABC) superfamily of transporters are found in all phyla including bacteria, plants, yeast, flies, fish, and mammals. All functional eukaryotic ABC transporters contain two ABCs and two transmembrane (TM) domains, each of which is composed of six TM α-helices, although additional TM helices are present in some transporters. ATP-binding cassette transporter G1 (ABCG1) promotes cholesterol efflux from cells and regulates intracellular cholesterol homeostasis. The mechanism of action of ABCG1 is controversial and it has been proposed to act at the plasma membrane to facilitate the efflux of cellular sterols to exogenous high-density lipoprotein (HDL). Here you can see a personal depiction of the recently published CryoEM structure of the human cholesterol transporter ABCG1 (PDB code: 7OZ1)
#molecularart ... #immolecular ... #ABCtransporter ... #membrane ... #cholesterol ... #ATPbinding ... #ABCG1 ... #cryoem
Rendered with @proteinimaging and finished with @corelphotopaint
#molecularart ... #immolecular ... #ABCtransporter ... #membrane ... #cholesterol ... #ATPbinding ... #ABCG1 ... #cryoem
Rendered with @proteinimaging and finished with @corelphotopaint
