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NMR analyses of the interactions of human annexin I with ATP, Ca 2+ , and Mg 2+
Author(s) -
Han Hee-Yong,
Lee Yeon-Hee,
Oh Jee-Young,
Na Doe-Sun,
Lee Bong-Jin
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00301-9
Subject(s) - annexin , annexin a2 , histidine , chemistry , binding site , amide , biochemistry , stereochemistry , biophysics , amino acid , biology , apoptosis
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 Ca 2+ , Mg 2+ , 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‐ 13 C, amide‐ 15 N) labeling technique was used to determine the interaction sites of Δ‐annexin I with Ca 2+ , Mg 2+ , and ATP. The 13 C 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.