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. Author manuscript; available in PMC: 2016 Sep 1.
Published in final edited form as: Trends Biochem Sci. 2015 Aug 5;40(9):526–534. doi: 10.1016/j.tibs.2015.07.002

Figure 4. Structural Basis of Slow Inactivation.

Figure 4

Specific structural features of NaVAb-WT and NaVRh, including a distorted selectivity filter and the breakdown of the four-fold symmetry of the pore, as expected for the slow inactivation state. Top panel: Close-up views of the extracellular entrance of NaVAb-I217C (green, symmetric), NaVAb-WT (grey, asymmetric), and NaVRh (salmon, collapsed) with semi-transparent surface representation of the three channels [9-11]. The high-strength-field site glutamate residue in each structure along with its nearby serine residue is shown in sticks. Bottom panel: Close-up view of the intracellular closed activation gate of NaVAb-I217C (symmetric, orange circle), NaVAb-WT (asymmetric, orange oval), and NaVRh (asymmetric, orange oval). .