Figure 1 - full size

 

Figure 1.
Figure 1. Schematic Representations of ALG-2 and Alix
Human ALG-2 has a Gly/Pro-rich N-terminal region followed by the PEF domain containing five EF-hands (EF1–EF5) with eight α helices (α1–α8). The first and second helices in each EF hand are alternatively named, for instance, helix E1 and helix F1, respectively. An alternatively spliced isoform (lacking Gly121-Phe122) is designated ALG-2^ΔGF122 in this article. Recombinant proteins of full-length ALG-2 and two types of N-terminal deletion mutants (des3-20ALG-2 and des3-23ALG-2) were crystallized. Alix has three distinct domains, named Bro1, V, and Pro-rich. A 16-mer synthetic oligopeptide of the ABS in Alix (Alix ABS peptide) was used for cocrystallization.

The above figure is reprinted by permission from Cell Press: Structure (2008, 16, 1562-1573) copyright 2008.