書誌事項
- タイトル別名
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- Molecular Basis of Alternating Access Membrane Transport by the Sodium-hydantoin Transporter Mhp1
- ヒダントイン ユソウタイ ニ ミル マク ユソウ キコウ ノ コウゾウ キバン
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Transporters are suggested to transport the substrates across the membrane using the alternating access mechanism in which the proteins have three functionally distinct conformational states, outward-facing, occluded and inward-facing. The structures from a secondary active transporter Mhp1 were recently determined in three states of the alternating access mechanism. Comparison of the structures shows that the conformational changes between these states are achieved by the rigid body movement of the four helices relative to the rest of the protein. The molecular basis of the alternating access mechanism is likely to be common among the LeuT superfamily.<br>
収録刊行物
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- 生物物理
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生物物理 51 (1), 004-009, 2011
一般社団法人 日本生物物理学会
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詳細情報 詳細情報について
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- CRID
- 1390282681511716352
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- NII論文ID
- 130000406422
- 10027414674
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- NII書誌ID
- AN00129693
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- ISSN
- 13474219
- 05824052
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- NDL書誌ID
- 10995333
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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
- Crossref
- CiNii Articles
- KAKEN
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- 抄録ライセンスフラグ
- 使用不可