NMR analyses of the interactions of human annexin I with ATP, Ca2+, and Mg2+

FEBS Letters

Lee, Bong-Jin¹  Na, Doe-Sun²  Oh, Jee-Young²  Lee, Yeon-Hee¹  Han, Hee-Yong¹ 

[1] Department of Pharmacy, Seoul National University, San 56-1, Shinlim-dong, Kwanak-ku, Seoul 151-742, South Korea;Department of Biochemistry, College of Medicine, University of Ulsan, 388-1 Pungnap-dong, Songpa-ku, Seoul, South Korea

关键词: Annexin I;    Ca2+;    Mg2+;    Adenosine triphosphate;    Nuclear magnetic resonance;   

DOI  :  10.1016/S0014-5793(98)00301-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Human annexin I is a member of the annexin family of calcium-dependent phospholipid binding proteins. The structure of an N-terminally truncated human annexin I (Δ-annexin I) and its interactions with Ca²⁺, Mg²⁺, and ATP were studied at the atomic level using nuclear magnetic resonance (NMR) spectroscopy. Since Δ-annexin I is a large protein, with a molecular weight of 35 kDa, a site-specific (carbonyl-¹³C, amide-¹⁵N) labeling technique was used to determine the interaction sites of Δ-annexin I with Ca²⁺, Mg²⁺, and ATP. The ¹³C NMR study focused on the carbonyl carbon resonances of the histidine residues of Δ-annexin I. We found that ATP binds to Δ-annexin I, and that the ATP binding site is located in the 1-domain of annexin I. We also found that histidine-52 is involved in that site, and that the binding ratio of ATP to Δ-annexin I is 1:1.

【 授权许可】

Unknown