The structure of human lipoprotein A-I - Evidence for the "belt" model"

被引：119

作者：

Koppaka, V

Silvestro, L

Engler, JA

Brouillette, CG

Axelsen, PH

机构：

[1] Univ Penn, Sch Med, Dept Pharmacol, Philadelphia, PA 19104 USA

[2] Univ Penn, Sch Med, Dept Med, Infect Dis Sect, Philadelphia, PA 19104 USA

[3] Univ Penn, Sch Med, Johnson Fdn Mol Biophys, Philadelphia, PA 19104 USA

[4] Univ Alabama, Med Ctr, Dept Biochem & Mol Genet, Birmingham, AL 35294 USA

[5] Univ Alabama, Med Ctr, Dept Physiol Opt, Ctr Macromol Crystallog, Birmingham, AL 35294 USA

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 1999年 / 274卷 / 21期

关键词：

D O I：

10.1074/jbc.274.21.14541

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：14541 / 14544

页数：4