par De Coen, Jean-Louis ;Deboeck, M.;Delcroix, Claude ;Lontie, Jean-Francois;Malmendier, Claude
Référence Proceedings of the National Academy of Sciences of the United States of America, 85, 15, page (5669-5672)
Publication Publié, 1988-08
Article révisé par les pairs
Résumé : The tertiary structure observed in the crystalline state for uteroglobin, a small steroid binding protein, is used as a template to build an approximated model for apolipoprotein A-II. The presence of four proline residues and four hydrophobic clusters located at similar positions in apolipoprotein A-II and uteroglobin is taken as the major source of stability in such tertiary structures. A brief description of plausible specific binding sites appearing on the model of apolipoprotein A-II is given. It is suggested that the internal cavity and the four surface pockets observed for uteroglobin and postulated for apolipoprotein A-II might be used to insure specific binding of triglycerides, phospholipids, or cholesterol.