Unknown

Dataset Information

0

The helix bundle: a reversible lipid binding motif.


ABSTRACT: Apolipoproteins are the protein components of lipoproteins that have the innate ability to inter convert between a lipid-free and a lipid-bound form in a facile manner, a remarkable property conferred by the helix bundle motif. Composed of a series of four or five amphipathic alpha-helices that fold to form a helix bundle, this motif allows the en face orientation of the hydrophobic faces of the alpha-helices in the protein interior in the lipid-free state. A conformational switch then permits helix-helix interactions to be substituted by helix-lipid interactions upon lipid binding interaction. This review compares the apolipoprotein high-resolution structures and the factors that trigger this switch in insect apolipophorin III and the mammalian apolipoproteins, apolipoprotein E and apolipoprotein A-I, pointing out the commonalities and key differences in the mode of lipid interaction. Further insights into the lipid-bound conformation of apolipoproteins are required to fully understand their functional role under physiological conditions.

SUBMITTER: Narayanaswami V 

PROVIDER: S-EPMC2808439 | biostudies-literature | 2010 Feb

REPOSITORIES: biostudies-literature

altmetric image

Publications

The helix bundle: a reversible lipid binding motif.

Narayanaswami Vasanthy V   Kiss Robert S RS   Weers Paul M M PM  

Comparative biochemistry and physiology. Part A, Molecular & integrative physiology 20090919 2


Apolipoproteins are the protein components of lipoproteins that have the innate ability to inter convert between a lipid-free and a lipid-bound form in a facile manner, a remarkable property conferred by the helix bundle motif. Composed of a series of four or five amphipathic alpha-helices that fold to form a helix bundle, this motif allows the en face orientation of the hydrophobic faces of the alpha-helices in the protein interior in the lipid-free state. A conformational switch then permits h  ...[more]

Similar Datasets

| S-EPMC2286553 | biostudies-literature
| S-EPMC8316464 | biostudies-literature
| S-EPMC2834481 | biostudies-literature
| S-EPMC390272 | biostudies-literature
| S-EPMC2761287 | biostudies-literature
| S-EPMC102627 | biostudies-literature
| S-EPMC2480675 | biostudies-literature
| S-EPMC2144225 | biostudies-other
2018-08-08 | GSE118239 | GEO
| S-EPMC3705624 | biostudies-literature