| Autor: |
De Coen, J L, Deboeck, M, Delcroix, C, Lontie, J F, Malmendier, C L |
| Zdroj: |
Proceedings of the National Academy of Sciences of the United States of America; August 1988, Vol. 85 Issue: 15 p5669-5672, 4p |
| Abstrakt: |
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. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
|
