Annexin A5 D226K structure and dynamics: identification of a molecular switch for the large‐scale conformational change of domain III
- 30 March 2001
- journal article
- Published by Wiley in FEBS Letters
- Vol. 493 (2-3) , 122-128
- https://doi.org/10.1016/s0014-5793(01)02285-2
Abstract
The domain III of annexin 5 undergoes a Ca2+- and a pH-dependent conformational transition of large amplitude. Modeling of the transition pathway by computer simulations suggested that the interactions between D226 and T229 in the IIID–IIIE loop on the one hand and the H-bond interactions between W187 and T224 on the other hand, are important in this process [Sopkova et al. (2000) Biochemistry 39, 14065–14074]. In agreement with the modeling, we demonstrate in this work that the D226K mutation behaves as a molecular switch of the pH- and Ca2+-mediated conformational transition. In contrast, the hydrogen bonds between W187 and T224 seem marginalKeywords
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