Fig. 3: Conformational changes during dimerization. | Nature Communications

Fig. 3: Conformational changes during dimerization.

From: Molecular architecture of black widow spider neurotoxins

Fig. 3

a Side-by-side comparison of α-LCT (compact state, sea green) and δ-LIT (extended state, extracted from the dimer, orange) superposed with α-LCT (transparent). b Front view of the ARD. Arrows indicate domain motion during dimerization. c Bottom views of the compact and extended states. The bottom part of the cylindrical (HBD) is exposed in the extended state. d Magnified view of the HBDs. The front helix (H7) is not shown for clarity. The H9a-H9b loop folds helically to complete H9 in the extended state. e Magnified view of the interface between the connector- and the AR-domain. f The schematic diagram illustrates the conformational change. PD:plug domain; HBD:helical bundle domain; CD: connector domain; ARD: ankyrin-like repeat domain.

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