Thermodynamics of apocalmodulin and nitric oxide synthase II peptide interaction
Thermodynamics of apocalmodulin and nitric oxide synthase II peptide interaction
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DOI：
10.1016/j.febslet.2004.10.048
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发表时间：
2004-11-19
期刊：
影响因子：
3.5
通讯作者：
Koch, KW
中科院分区：
文献类型：
--
作者：
Censarek, P;Beyermann, M;Koch, KW
钙调素（CaM）的无钙形式，apocal-modulin（ApoCaM），调节多种靶蛋白，包括一氧化氮合酶II（NOS-II）。NOS-II的CaM结合位点可以高亲和力结合ApoCaM。在CaM结合基序的关键位置3、9和13处用带电氨基酸取代疏水氨基酸并没有消除ApoCaM相互作用，尽管这种相互作用的亲和力显著降低。等温滴定量热法显示，ApoCaM和合成的NOS-II肽的相互作用是熵驱动的。(C)2004年由Elsevier B. V.代表欧洲生物化学学会联合会出版。
The Ca2+-free form of calmodulin (CaM), apocal-modulin (ApoCaM), regulates a variety of target proteins including nitric oxide synthase II (NOS-II). The CaM-binding site of NOS-II can bind ApoCaM with high affinity. Substitution of hydrophobic amino acids by charged amino acids at crucial positions 3, 9 and 13 within the CaM-binding motif did not abolish the ApoCaM interaction that occurred with significant affinity, though the affinity of the interaction was decreased remarkably. Isothermal titration calorimetry revealed that interaction of ApoCaM and synthetic NOS-II peptides was driven entropically. (C) 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.