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Function
Disease
an between them. The stability of the 4D motif is attributed to adjacent positively charged residues (Lys325, Arg388, and Arg517), forming stabilizing salt bridges, leading to the newly named (four acidic residues stabilized by three basic residues).
The study also identified additional metal-binding sites (His264 and His471 sites) in TcAChE through crystallographic analysis, but these appear to be weaker or crystallographic artifacts. Using metadynamics and molecular dynamics (MD) simulations with quantum potentials (QM/MM-MD), the binding strength of metal cations at the 4D site was compared to that of the 4D site in human fibrin-stabilizing factor (fXIIIa), which lacks stabilizing cationic residues. Results showed that while TcAChE’s 4A/3B motif maintains structural integrity upon metal binding/unbinding, the is stable in presence of a metal ion but without a metal ions due to electrostatic repulsion. This is seen clearly in an
between these two states.
Relevance
Structural highlights
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