title: Lipid-free apoA-I structure - Origins of model diversity.
abstract: Apolipoprotein A-I (apoA-I) is a prominent member of the exchangeable apolipoprotein class of proteins, capable of transitioning between lipid-bound and lipid-free states. It is the primary structural and functional protein of high density lipoprotein (HDL). Lipid-free apoA-I is critical to de novo HDL formation as it is the preferred substrate of the lipid transporter, ATP Binding Cassette Transporter A1 (ABCA1) Remaley et al. (2001) [1]. Lipid-free apoA-I is an important element in reverse cholesterol transport and comprehension of its structure is a core issue in our understanding of cholesterol metabolism. However, lipid-free apoA-I is highly conformationally dynamic making it a challenging subject for structural analysis. Over the past 20years there have been significant advances in overcoming the dynamic nature of lipid-free apoA-I, which have resulted in a multitude of proposed conformational models.
authors.affiliation: Children's Hospital Oakland Research Institute, Oakland, CA 94609, United States. Electronic address: moda@chori.org.
authors.forename: Michael N
authors.initials: MN
authors.lastname: Oda
mesh_terms: D064286:ATP Binding Cassette Transporter 1 / Q000378:metabolism; D016632:Apolipoprotein A-I / Q000737:chemistry* / Q000378:metabolism*; D001692:Biological Transport / Q000502:physiology; D002784:Cholesterol / Q000378:metabolism; D006801:Humans; D050356:Lipid Metabolism / Q000502:physiology; D008055:Lipids / Q000737:chemistry*
chemical_list: D064286:ATP Binding Cassette Transporter 1; D016632:Apolipoprotein A-I; D008055:Lipids; D002784:Cholesterol
keywords: Apolipoprotein A-I; High density lipoprotein cholesterol; Protein structure