The structure of dimeric apolipoprotein A-IV and its mechanism of self-association.
The structure of dimeric apolipoprotein A-IV and its mechanism of self-association.
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DOI:
10.1016/j.str.2012.02.020
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发表时间:
2012-05-09
期刊:
影响因子:
5.7
通讯作者:
Thompson, Thomas B.
中科院分区:
文献类型:
--
作者:
Deng, Xiaodi;Morris, Jamie;Dressmen, James;Tubb, Matthew R.;Tso, Patrick;Jerome, W. Gray;Davidson, W. Sean;Thompson, Thomas B.
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 (HDL). 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.
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DOI:
10.1073/pnas.83.22.8457
发表时间:
1986-11-01
影响因子:
11.1
作者:
KARATHANASIS, SK;OETTGEN, P;ANTONARAKIS, SE
通讯作者:
ANTONARAKIS, SE
DOI:
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发表时间:
1997-11-11
影响因子:
11.1
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通讯作者:
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DOI:
10.1016/0005-2760(95)00228-6
发表时间:
1996-03-29
期刊:
BIOCHIMICA ET BIOPHYSICA ACTA-LIPIDS AND LIPID METABOLISM
影响因子:
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作者:
Main, LA;Ohnishi, T;Yokoyama, S
通讯作者:
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影响因子:
4.8
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通讯作者:
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DOI:
10.1016/0005-2760(83)90040-1
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1983-01-01
期刊:
BIOCHIMICA ET BIOPHYSICA ACTA
影响因子:
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作者:
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FORTE, TM