Figure 3 - full size

 

Figure 3.
Fig. 3. The overall conformation of Impβ in complex with IBB[SPN1] and IBB[α], respectively, differs significantly. (a) Superposition of the structures of Impβ/IBB[SPN1] (blue) and Impβ/IBB[α] (red). Only Impβ is shown in each case. The superposition reveals a considerable difference of 14 Å in the dilatation of both molecules. The distances between Asn141 and Ala876 were measured and are indicated. (b) Comparison between a homology amino acid sequence alignment^17 and a structure-based sequence alignment of IBB[α] and IBB[SPN1] derived from the crystal structures of Impβ/IBB[α] and Impβ/IBB[SPN1]: Green boxes indicate functionally conserved residues regarding interaction with Impβ; red boxes mark residues of IBB[α] that interact with the acidic loop of Impβ. They also mark the corresponding amino acids of IBB[SPN1] according to Ref. 9.

The above figure is reprinted by permission from Elsevier: J Mol Biol (2007, 374, 1129-1138) copyright 2007.