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Fig. 1. Models of human PD-associated proteins. (A) -Synuclein is a 140 amino acid protein belonging to a family of related synucleins that includes β- and -synuclein. It has an N-terminal amphipathic region containing six imperfect repeats with a KTKEGV consensus sequence, a hydrophobic central region that contains the non-amyloid-β component (NAC) domain, and a highly acidic C-terminal tail containing several phosphorylation sites. (B) Parkin is a 465 amino acid protein that functions as an E3 ubiquitin ligase. It contains an N-terminal ubiquitin-like (UBL) domain that binds to RPN10 subunit of the 26S proteasome system, a central linker region, and a C-terminal RING domain comprising two RING finger motifs (RING1 and RING2) separated by an in-between-RING (IBR) domain. (C) DJ-1 is a highly conserved 189 amino acid protein that is ubiquitously and abundantly expressed in most mammalian tissues and belongs to the DJ-1/ThiJ/PfpI superfamily. (D) PINK1 is a highly conserved 581 amino acid protein that is ubiquitously expressed. It localizes to the mitochondria via an N-terminal mitochondrion-targeting motif (MTS). Furthermore, it shares sequence similarity with Ca²⁺/calmodulin-dependent protein kinase I and contains a catalytic serine/threonine kinase domain. (E) LRRK2 is a 2537 amino acid complex multi-domain protein that consists of a ankyrin-repeat region (ANK), an N-terminal leucine-rich repeat domain (LRR), a GTPase Roc domain (Roc) followed by associated C terminal of Roc (COR), a mitogen-activated kinase kinase kinase domain, and C-terminal WD40 repeat (approximately 40 amino acid repeats that form a β-propeller structure that might serve as a rigid scaffold for protein interactions). Approximate positions of missense mutations causing PD are indicated with arrows.

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