A new way for sterols to walk on water.
The crystal structure of a homolog of oxysterol binding protein solved by Jim Hurley and coworkers (Im et al., 2005) shows that this large family acts as cholesterol transporters, taking not only the lipid but also large numbers of water molecules into an internal pocket.
Levine
Tim
T
Division of Cell Biology, Institute of Ophthalmology, Bath Street, London EC1V 9EL, United Kingdom.
D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism; D011987:Receptors, Steroid / Q000235:genetics / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013261:Sterols / Q000737:chemistry*; D014867:Water / Q000737:chemistry*; D000098825:Oxysterol Binding Proteins
D005656:Fungal Proteins; D008565:Membrane Proteins; D010940:Plant Proteins; D011987:Receptors, Steroid; D029701:Saccharomyces cerevisiae Proteins; D013261:Sterols; D014867:Water; C087901:KES1 protein, S cerevisiae; D000098825:Oxysterol Binding Proteins