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FEBS Lett. 2001 Mar 30;493(2-3):122-8.

Annexin A5 D226K structure and dynamics: identification of a molecular switch for the large-scale conformational change of domain III.

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  • 1UFR des Sciences Pharmaceutiques, 5 rue Vaubenard, F-14032 Caen, France.


The domain III of annexin 5 undergoes a Ca(2+)- 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 Ca(2+)-mediated conformational transition. In contrast, the hydrogen bonds between W187 and T224 seem marginal.

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