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Proposed folding pattern for apolipoprotein A-II based on a structural analogy with uteroglobin.

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

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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.