In:
FEBS Letters, Wiley, Vol. 425, No. 3 ( 1998-04-03), p. 523-527
Abstract:
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.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/S0014-5793(98)00301-9
Language:
English
Publisher:
Wiley
Publication Date:
1998
detail.hit.zdb_id:
1460391-3
SSG:
12
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