Molecular Dynamics Study of α-Synuclein Domain Deletion Mutant Monomers.

ABSTRACT: Aggregates of misfolded α-synuclein proteins are key markers of Parkinson's disease. The protein α-synuclein (aSyn) is an intrinsically disordered protein (IDP) and therefore lacks a single stable 3D structure, instead sampling multiple conformations in solution. It is primarily located in presynaptic terminals and is thought to help regulate synaptic vesicle trafficking and neurotransmitter release. ASyn proteins have three domains: an N-terminal domain, a hydrophobic non-amyloid-β component (NAC) core implicated in aggregation, and a proline-rich C-terminal domain. Asyn proteins with truncated C-terminal domains are known to be prone to aggregation and suggest that understanding domain-domain interactions in aSyn monomers could help elucidate the role of the flanking domains in modulatin

SUBMITTER: Onishi N 

PROVIDER: S-EPMC12650653 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature