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. 2017 May 5;12(5):e0177077. doi: 10.1371/journal.pone.0177077

Fig 6. The model of APHC1 binding with TRPV1 outer region.

Fig 6

A, Aligned sequences of APHC1 and trypsin inhibitor SHPI-1. B, Different views on the minimal-energy complex calculated for APHC1 and close stated TRPV1. Backbone of APHC1 is shown magenta, backbone of the channel is colored green. The C-terminal helix of the APHC1 intercalates between diverging P-loops. C, The details of polypeptide-channel interaction. Key residues involved in the interaction are shown as sticks. D, Superimposition of two APHC1 binding models—APHC1—closed TRPV1 (green and magenta) and APHC1—opened TRPV1 (cyan and orange). In the open state the slot between P-loops is narrower and APHC1 is shifted in the external direction.