3S84

Dimeric apoA-IV

Summary for 3S84

• Entry DOI: 10.2210/pdb3s84/pdb
• Descriptor: Apolipoprotein A-IV, SULFATE ION (3 entities in total)
• Functional Keywords: four helix bundle, transport protein
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P06727
• Total number of polymer chains: 2
• Total formula weight: 63330.95

Authors

Deng, X.,Davidson, W.S.,Thompson, T.B. (deposition date: 2011-05-27, release date: 2012-05-16, Last modification date: 2024-02-28)

Primary citation

Deng, X.,Morris, J.,Dressmen, J.,Tubb, M.R.,Tso, P.,Jerome, W.G.,Davidson, W.S.,Thompson, T.B.
The Structure of Dimeric Apolipoprotein A-IV and Its Mechanism of Self-Association.
Structure, 20:767-779, 2012

PubMed Abstract: Apolipoproteins are key structural elements of lipoproteins and critical mediators of lipid metabolism. Their detergent-like properties allow them to emulsify lipid or exist in a soluble lipid-free form in various states of self-association. Unfortunately, these traits have hampered high-resolution structural studies needed to understand the biogenesis of cardioprotective high-density lipoproteins (HDLs). We derived a crystal structure of the core domain of human apolipoprotein (apo)A-IV, an HDL component and important mediator of lipid absorption. The structure at 2.4 Å depicts two linearly connected 4-helix bundles participating in a helix swapping arrangement that offers a clear explanation for how the protein self-associates as well as clues to the structure of its monomeric form. This also provides a logical basis for antiparallel arrangements recently described for lipid-containing particles. Furthermore, we propose a "swinging door" model for apoA-IV lipid association.

PubMed: 22579246
DOI: 10.1016/j.str.2012.02.020

Experimental method

X-RAY DIFFRACTION (2.4 Å)