A Structural Proteomics Exploration of Synphilin-1 and Alpha-Synuclein Interaction in Pathogenesis of Parkinson's Disease.

ABSTRACT: Pathological significance of interaction of Synphilin-1 with mutated alpha-synuclein is well known to have serious consequences in causing the formation of inclusion bodies that are linked to Parkinson's disease (PD). Information extracted so far pointed out that specific mutations, A53T, A30P, and E46K, in alpha-synuclein promote such interactions. However, a detailed structural study of this interaction is pending due to the unavailability of the complete structures of the large protein Synphilin-1 of chain length 919 residues and the mutated alpha-synuclein having all the reported specific mutations so far. In this study, a semi-automatic pipeline-based meta-predictor, AlphaLarge, is created to predict high-fidelity structures of large proteins like Synphilin-1 given the limitations of

SUBMITTER: Tripathi A 

PROVIDER: S-EPMC11674031 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature