Proposed Folding Pattern for Apolipoprotein A-II Based on a Structural Analogy with Uteroglobin

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...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1988-08, Vol.85 (15), p.5669-5672
Main Authors: De Coen, Jean-Louis, Deboeck, Michel, Delcroix, Claude, Lontie, Jean-Francois, Malmendier, Claude L.
Format: Article
Language:English
Subjects:
Amino acids
Animals
Apolipoprotein A-II
Apolipoproteins A - metabolism
Binding Sites
Chemical Phenomena
Chemistry
Cholesterol - metabolism
Crystallization
Dimers
Disulfides
Glycoproteins - metabolism
Humans
Lipids
Lipoproteins, HDL - metabolism
Models, Molecular
Molecular structure
Molecules
Monomers
Phospholipids
Phospholipids - metabolism
Protein Conformation
Rabbits
Steroids
Templates, Genetic
Triglycerides - metabolism
uteroglobin
Uteroglobin - metabolism
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Summary: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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.85.15.5669