FIGURE 1
FROM:
The mitochondrial serine protease HtrA2/Omi: an overview
L Vande Walle, M Lamkanfi and P Vandenabeele
BACK TO ARTICLEFigure 1.

Domain organization and phylogenetic analysis of human HtrA2/Omi. (a) Full-length HtrA2/Omi consists of five functional domains and motifs: the N-terminal mitochondrial localization signal (MLS), the transmembrane (TM) segment, the IAP-binding motif (IBM), the serine protease domain and the C-terminal PDZ domain. Amino-acid substitutions associated with Parkinson's disease and the Parkinsonian phenotype of the Mnd2 mice are indicated below the functional domains in italic and bold, respectively. The catalytic triad residues are depicted above the functional domains. (b) Phylogenetic relationship of the HtrA family members. The sequences were aligned using the CLUSTAL X (gap weight=10.00; gap length weight=0.20) and trees were visualized in TreeCon. Bt, Bos taurus; Cf, Canis familiaris; Dm, Drosophila melanogaster; Ec, Escherichia coli; Hs, Homo sapiens; Mm, Mus musculus; Mu, Macaca mulatta; Rn, Rattus norvegicus; Xt, Xenopus tropicalis
