Figure 1: Organization of Hippi and Hip-1. | Nature Cell Biology

Figure 1: Organization of Hippi and Hip-1.

From: Recruitment and activation of caspase-8 by the Huntingtin-interacting protein Hip-1 and a novel partner Hippi

Figure 1

a, Schematic diagram of Hippi and Hip-1. Coiled-coil-forming domains are predicted but not shown. Predicted domains, including a leucine zipper, the talin-like domain and the pseudo death-effector domain (pDED) in Hip-1, and the myosin-like domain and the pDED in Hippi are shown. b, c, The pDED of Hippi and its amino-acid sequence homology to other death-effector domains. The entire amino-acid sequences of the Hippi pDED and other known DEDs are shown. The first and last amino acids of each DED in their respective proteins are indicated on the left and right of each sequence. The region corresponding to the fifth helix (α5) is indicated. The arrowhead in c indicates the position of the critical amino acid that distinguishes the first group of DEDs, which have a charged residue (K) at this position, from the second group, which have largely hydrophobic residues (L, V) at the equivalent position.

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