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- 田中 将史
- 神戸薬科大学 薬品物理化学研究室
書誌事項
- タイトル別名
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- Conformation of Apolipoprotein A-I and Its Interaction with Lipid Membrane
- ApoA I ノ コウゾウ ト シシツマク トノ ソウゴ サヨウ
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抄録
Interaction of apolipoprotein (apo) A-I with lipid membrane is involved in a large number of processes in lipoprotein metabolism and cholesterol homeostasis. This review discusses the molecular mechanisms of interaction of apoA-I with lipid membrane in view of their structures. Lipid-free apoA-I is folded into two domains, comprising an Nterminal part forming a four-helix bundle and a discrete C-terminal part. It is well known that insertion of a proline residue into a protein sequence disruptsα-helix structure. Perturbation of the helix bundle structure occurs by the proline insertion into the putative helical region in the N-terminal domain, suggesting that the substituted residue is part of the helix bundle. In lipid-binding, apoA-I recognizes headgroup separation (hydrated space) between phospholipid molecules at the lipid membrane. ApoA-I initially binds to lipid through the C-terminal domain, followed by a conformational opening of the helix bundle with an accompanying increase inα-helical content. The transition from random coil toα-helix has been shown to produce a large negative enthalpy (exothermic heat) that drives lipid binding. Despite a lack of the C-terminal domain, which is critical for lipid-binding, perturbation of the helix bundle structure restored the lipidbinding ability by exposing a potential lipid-binding region in the N-terminal domain.
収録刊行物
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- 膜
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膜 32 (5), 253-258, 2007
日本膜学会
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詳細情報 詳細情報について
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- CRID
- 1390282681398092544
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- NII論文ID
- 10019834069
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- NII書誌ID
- AN0023215X
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- ISSN
- 18846440
- 03851036
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- NDL書誌ID
- 8960968
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- 本文言語コード
- ja
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- データソース種別
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- JaLC
- NDL
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- 抄録ライセンスフラグ
- 使用不可