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Importantly, it is also likely that this process will be invaluable in the characterisation of various S mutations implicated in PD. Any benefit that recent studies have obtained in modifying the native state of the protein has been conclusively demonstrated by the limited success of the instances where this approach has been used dogmatically to generate a robust and informative alteration.
The heterogeneity of S is not likely to limit its pathophysiological role to the aggregation of S in an amyloid form. In fact, protein-protein interactions are a likely component of the native state of the protein [29] and this will need to be characterized as part of the overall native state characterization, as studies routinely fail to consider protein-protein interactions.[47] In fact, several studies have reported that binding partners to S can affect the S conformational ensemble, and that this may play a crucial role in PD pathogenesis.
Given the considerable work that has been performed to date on one of the most studied proteins in PD, it is perhaps surprising that, despite the wealth of literature, S–native structural information still remains relatively under-developed, even compared to other human proteins that have been studied. In this issue, the first definitive structure of full-length S extracted from the cytoplasmic inclusion packets seen in the brains of familial PD patients, and the crystal structure of S N-terminal, have been reported [38]. Remarkably, this represents the first resolved native structure obtained for the full-length protein.
There are no known key interacting partners or post-translational modifications for native S, which has further complicated the characterization of the native state, particularly in vivo. However, the recent report of several key interacting partners (see Toolbox; associated with the intrinsic disorder database), provides a starting point to characterize the molecular role of full-length native S and assess potential modulation.
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