TY - JOUR
T1 - Dynamic structural flexibility of α-synuclein.
AU - Mor, Danielle Emille
AU - Ugras, Scott E
AU - Daniels, Malcolm J
AU - Ischiropoulos, Harry
PY - 2015/12/31
Y1 - 2015/12/31
N2 - α-Synuclein is a conserved, abundantly expressed protein that is partially localized in pre-synaptic terminals in the central nervous system. The precise biological function(s) and structure of α-synuclein are under investigation. Recently, the native conformation and the presence of naturally occurring multimeric assemblies have come under debate. These are important deliberations because α-synuclein assembles into highly organized amyloid-like fibrils and non-amyloid amorphous aggregates that constitute the neuronal inclusions in Parkinson's disease and related disorders. Therefore understanding the nature of the native and pathological conformations is pivotal from the standpoint of therapeutic interventions that could maintain α-synuclein in its physiological state. In this review, we will discuss the existing evidence that define the physiological states of α-synuclein and highlight how the inherent structural flexibility of this protein may be important in health and disease.
AB - α-Synuclein is a conserved, abundantly expressed protein that is partially localized in pre-synaptic terminals in the central nervous system. The precise biological function(s) and structure of α-synuclein are under investigation. Recently, the native conformation and the presence of naturally occurring multimeric assemblies have come under debate. These are important deliberations because α-synuclein assembles into highly organized amyloid-like fibrils and non-amyloid amorphous aggregates that constitute the neuronal inclusions in Parkinson's disease and related disorders. Therefore understanding the nature of the native and pathological conformations is pivotal from the standpoint of therapeutic interventions that could maintain α-synuclein in its physiological state. In this review, we will discuss the existing evidence that define the physiological states of α-synuclein and highlight how the inherent structural flexibility of this protein may be important in health and disease.
UR - https://europepmc.org/articles/PMC4758871
U2 - 10.1016/j.nbd.2015.12.018
DO - 10.1016/j.nbd.2015.12.018
M3 - Article
C2 - 26747212
SN - 0969-9961
VL - 88
SP - 66
EP - 74
JO - Neurobiology of Disease
JF - Neurobiology of Disease
ER -