Proc Natl Acad Sci U S A. 1997 Nov 11;94(23):12291-6.

Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation.

Borhani DW, Rogers DP, Engler JA, Brouillette CG.

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Department of Organic Chemistry, Southern Research Institute, Birmingham, AL 35205, USA. borhani@sri.org

Abstract

The structure of truncated human apolipoprotein A-I (apo A-I), the major protein component of high density lipoprotein, has been determined at 4-A resolution. The crystals comprise residues 44-243 (exon 4) of apo A-I, a fragment that binds to lipid similarly to intact apo A-I and that retains the lipid-bound conformation even in the absence of lipid. The molecule consists almost entirely of a pseudo-continuous, amphipathic alpha-helix that is punctuated by kinks at regularly spaced proline residues; it adopts a shape similar to a horseshoe of dimensions 125 x 80 x 40 A. Four molecules in the asymmetric unit associate via their hydrophobic faces to form an antiparallel four-helix bundle with an elliptical ring shape. Based on this structure, we propose a model for the structure of apo A-I bound to high density lipoprotein.

PMID:: 9356442; [PubMed - indexed for MEDLINE]
PMCID: PMC24911

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Structures reported by this article

Crystal Structure Of Human Apolipoprotein A-I

PDB: 1AV1

Source: Homo sapiens

Method: X-Ray Diffraction

Resolution: 4 Å

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