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. 2016 May 26;165(6):1467–1478. doi: 10.1016/j.cell.2016.05.022

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© 2016 Elsevier Inc.

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Figure S6 — Examination of the Interactions between hNPC1 and the Cleaved Glycoprotein of Ebola Virus (EBOV-GPcl), Related to Figure 5

(A) There is very weak, if any, binding between isolated hNPC1(NTD) and EBOV-GPcl. The binding affinity was measure by SPR. Please refer to Supplemental Experimental Procedures for details.

(B) Modeling of the EBOV-GPcl trimer bound to three hNPC1. When three FL hNPC1 molecules are docked to the structure of trimeric EBOV-GPcl in complex with three domain C as rigid body (PDB: 5F1B), the TMD of the three hNPC1 protomers are out of the same plane. TM1 in each protomer collides with TM3 in the adjacent one.