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Stabilization of the alpha 2 Isoform of Na,K-ATPase by Mutations in a Phospholipid Binding Pocket

  作者 Kapri-Pardes, E; Katz, A; Haviv, H; Mahmmoud, Y; Ilan, M; Khalfin-Penigel, I; Carmeli, S; Yarden, O; Karlish, SJD  
  选自 期刊  Journal of Biological Chemistry;  卷期  2011年286-50;  页码  42888-42899  
  关联知识点  
 

[摘要]Background: The alpha 2 isoform of Na, K-ATPase is unstable compared with alpha 1 and alpha 3. Results: Mutations in TM8-10 strongly stabilize alpha 2. A novel phospholipid antagonist selectively inactivates alpha 2, and mutations in TM8-10 protect against inactivation. Conclusion: A phosphatidylserine binding pocket within TM8-10 has been identified. Significance: Mechanistic insights into alpha 2 instability and a possible physiological role have been obtained.

 
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