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. 2017 Oct 24;6:e31054. doi: 10.7554/eLife.31054

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© 2017, Martin et al

This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited.

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Figure 6. — (A) Ribbon diagram of SUR1 showing location of GBC, which is primarily coordinated by the inner helices of TMD1 (purple) and TMD2 (cyan). (B) Slice view of model in (A) viewed from the extracellular side. Note juxtaposition of L0 to helices in ABC core directly interacting with GBC. (C) Close-up of GBC binding pocket, showing all residues which immediately line the pocket and seem to form direct contact with GBC; a subset of these residues were mutated to test their role in GBC binding (Figure 7). (D) Magnified view in (B), highlighting indirect roles of Y230 and W232 (L0) in GBC binding. These both likely stabilize interactions between residues on helix 16 of TMD2 and GBC, at the same time anchoring this helix of L0 to the ABC core structure.

Figure 6—figure supplement 1. — (A) Ribbon diagram of SUR1 showing location of GBC, which is primarily coordinated by the inner helices of TMD1 (purple) and TMD2 (cyan). (B) Slice view of model in (A) viewed from the extracellular side. Note juxtaposition of L0 to helices in ABC core directly interacting with GBC. (C) Close-up of GBC binding pocket, showing all residues which immediately line the pocket and seem to form direct contact with GBC; a subset of these residues were mutated to test their role in GBC binding (Figure 7). (D) Magnified view in (B), highlighting indirect roles of Y230 and W232 (L0) in GBC binding. These both likely stabilize interactions between residues on helix 16 of TMD2 and GBC, at the same time anchoring this helix of L0 to the ABC core structure.