| Autor: |
Takaharu Sakuragi, Shigekazu Nagata, Ryuta Kanai, E. Onishi, Akihisa Tsutsumi, Akiko Nakagawa, Chikashi Toyoshima, H. Narita, Masahide Kikkawa, Takeshi Baba, T. Miyazaki |
| Rok vydání: |
2021 |
| Předmět: |
|
| DOI: |
10.1101/2021.05.06.442885 |
| Popis: |
Xkr8-Basigin is a phospholipid scramblase at plasma membranes that is activated by kinase or caspase. We investigated its structure at a resolution of 3.8Å. Its membrane-spanning region had a cuboid-like structure stabilized by salt bridges between hydrophilic residues in helices in the lipid layer. The molecule carried phosphatidylcholine in a cleft on the surface that may function as an entry site for phospholipids. Five charged residues placed from top to bottom inside the molecule were essential for providing a path for scrambling phospholipids. A tryptophan residue was present at the extracellular end of the pathway and its mutation made the Xkr8-Basigin complex constitutively active, indicating its function as a gatekeeper. The structure of Xkr8-Basigin provides novel insights into the molecular mechanisms underlying phospholipid scrambling. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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