Fig. 2

Comparison of the cryo-EM structure of IRΔβ-zipInsFv with the crystal structure of apo IRΔβ. a Domain arrangement in apo IRΔβ (left) with domains colored as in Fig. 1a. b Apo IRΔβ but with only domains L1, CR, L2, L1′, CR′, and αCT′ shown in color (for comparison with panel (d)). c Domain arrangement in IRΔβ-zipInsFv with domains colored as in Fig. 1a. d IRΔβ-zipInsFv but with only domains L1, CR, L2, L1′, CR′, and αCT′ shown in color in order to highlight the rearrangement of the insulin-bound (L1-CR-L2) + αCT′ module with respect to apo IRΔβ (panel (b)). e Comparison of the relative disposition of domains FnIII and FnIII′ in apo IRΔβ (grey) and in IRΔβ-zipInsFv (colored). f Pseudo-two-fold-symmetric interaction of domains FnIII-3 and FnIII-3′ within IRΔβ-zipInsFv. For clarity, only one member of each pseudo-symmetry-related residue pair is labeled. Green arrows in all panels indicate the direction of membrane entry. Panel (a) is adapted from Fig. 1a of Xu et al.²²