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J Biol Chem, Vol. 274, Issue 21, 14541-14544, May 21, 1999

COMMUNICATION
The Structure of Human Lipoprotein A-I
EVIDENCE FOR THE "BELT" MODEL

Vishwanath Koppaka, Loraine Silvestro, Jeffrey A. Engler^§, Christie G. Brouillette^§¶, and Paul H. Axelsen

From the  Department of Pharmacology,  Department of Medicine, Infectious Diseases Section, and the Johnson Foundation for Molecular Biophysics, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104-6084 and the ^§ Department of Biochemistry and Molecular Genetics and ^¶ Department of Physiological Optics, Center for Macromolecular Crystallography, University of Alabama at Birmingham Medical Center, Birmingham, Alabama 35294

The two main competing models for the structure of discoidal lipoprotein A-I complexes both presume that the protein component is helical and situated around the perimeter of a lipid bilayer disc. However, the more popular "picket fence" model orients the protein helices perpendicular to the surface of the lipid bilayer, while the alternative "belt" model orients them parallel to the bilayer surface. To distinguish between these models, we have investigated the structure of human lipoprotein A-I using a novel form of polarized internal reflection infrared spectroscopy that can characterize the relative orientation of protein and lipid components in the lipoprotein complexes under native conditions. Our results verify lipid bilayer structure in the complexes and point unambiguously to the belt model.

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Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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