The preincubated ATP-Zn 2+ -rhNGF mixture resulted in a clear trend towards a decrease of the affinity to either TrkA (K D = 0.89 nM) or p75 NTR (K D = 3.20 nM) with respect to rhNGF alone (TrkA K D = 0.16 nM; p75 NTR K D = 0.83 nM) and confirmed a more pronounced effect on TrkA than on p75 NTR receptor’s binding. 4 Discussion The present study by integrative structural biology, combining multiple experimental techniques, unveiled the binding cartography of ATP to rhNGF, aiming at the structural and functional characterization of new endogenous modulators of NGF biological activity.
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Endogenous modulators of neurotrophin signaling: Landscape of the transient ATP-NGF interactions.
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