IndraLab

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KCNMA1 binds full-length NADase. 2 / 2
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"The affinity of binding between SLO and full-length NADase, as determined by BLI steady-state analysis, was 8-fold higher (K D, 2.584 muM) than the affinity of SLO for NADase lacking the N-terminal translocation domain (190NADase; K D, 20.65 muM)."
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"Structural characterization of the full-length NADase/SLO complex by combined use of X-ray crystallography, computational modeling, and small-angle scattering reveals an ensemble of a compact and an extended states (Fig. 3)."
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