Part:BBa_K5079030
Protein Switch 5 (K_45_WT)
In an SDS-PAGE analysis of an enzymatic assay, MS5 demonstrated the production of α-synuclein fragments overtime consistently across both Trial 1 and Trial 2. The observed fragment had an approximate molecular weight of 10 kDa, suggesting cleavage likely occurred near the C-terminus of α-synuclein, possibly at residues D115 or N122. This hypothesis is supported by the fact that KLK6 was inserted into cyclophilin D (Cyp-D) at position K45 in the MS5 variant. K45 is a highly conserved residue among Cyp-D homologs, and its modification may have disrupted the native binding affinity between Cyp-D and α-synuclein. If Cyp-D’s binding to α-synuclein is impaired while KLK6's proteolytic activity remains intact, cleavage at the C-terminus of α-synuclein would be anticipated, which aligns with the experimental observations.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BamHI site found at 785
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
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