3R2P

2.2 Angstrom Crystal Structure of C Terminal Truncated Human Apolipoprotein A-I Reveals the Assembly of HDL by Dimerization.

Summary for 3R2P

• Entry DOI: 10.2210/pdb3r2p/pdb
• Descriptor: Apolipoprotein A-I (2 entities in total)
• Functional Keywords: amphipathic alpha-helix, major protein of high density lipoprotein (hdl), lipid binding, plasma, lipid transport
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P02647
• Total number of polymer chains: 1
• Total formula weight: 21656.23

Authors

Mei, X.,Atkinson, D. (deposition date: 2011-03-14, release date: 2011-09-21, Last modification date: 2024-04-03)

Primary citation

Mei, X.,Atkinson, D.
Crystal Structure of C-terminal Truncated Apolipoprotein A-I Reveals the Assembly of High Density Lipoprotein (HDL) by Dimerization.
J.Biol.Chem., 286:38570-38582, 2011

PubMed Abstract: Apolipoprotein A-I (apoA-I) plays important structural and functional roles in plasma high density lipoprotein (HDL) that is responsible for reverse cholesterol transport. However, a molecular understanding of HDL assembly and function remains enigmatic. The 2.2-Å crystal structure of Δ(185-243)apoA-I reported here shows that it forms a half-circle dimer. The backbone of the dimer consists of two elongated antiparallel proline-kinked helices (five AB tandem repeats). The N-terminal domain of each molecule forms a four-helix bundle with the helical C-terminal region of the symmetry-related partner. The central region forms a flexible domain with two antiparallel helices connecting the bundles at each end. The two-domain dimer structure based on helical repeats suggests the role of apoA-I in the formation of discoidal HDL particles. Furthermore, the structure suggests the possible interaction with lecithin-cholesterol acyltransferase and may shed light on the molecular details of the effect of the Milano, Paris, and Fin mutations.

PubMed: 21914797
DOI: 10.1074/jbc.M111.260422

Experimental method

X-RAY DIFFRACTION (2.2045 Å)