1AV1

CRYSTAL STRUCTURE OF HUMAN APOLIPOPROTEIN A-I

Summary for 1AV1

• Entry DOI: 10.2210/pdb1av1/pdb
• Descriptor: APOLIPOPROTEIN A-I (1 entity in total)
• Functional Keywords: lipoprotein, lipid transport, cholesterol metabolism, atherosclerosis, hdl, lcat-activation
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P02647
• Total number of polymer chains: 4
• Total formula weight: 93762.24

Authors

Borhani, D.W.,Rogers, D.P.,Engler, J.A.,Brouillette, C.G. (deposition date: 1997-09-23, release date: 1998-02-04, Last modification date: 2024-02-07)

Primary citation

Borhani, D.W.,Rogers, D.P.,Engler, J.A.,Brouillette, C.G.
Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation.
Proc.Natl.Acad.Sci.USA, 94:12291-12296, 1997

PubMed 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.

PubMed: 9356442
DOI: 10.1073/pnas.94.23.12291

Experimental method

X-RAY DIFFRACTION (4 Å)