Overlap between aggregation prone and T-cell autoimmune epitope regions in human amyloidogenic proteins.
Human amyloidogenic proteins whose amino acid sequences contain experimentally validated aggregating peptides (bold font) as well as experimentally validated T-cell autoimmune epitope peptides (underlined) are shown. All available experimental data on these proteins is consolidated into the regions highlighted in the sequences. The PDB26 was queried for available structural information on these proteins and information obtained was used to map overlapping aggregation prone and autoimmune epitope regions in the respective protein structures. These regions are shown in magenta. The magenta regions in structural images correspond to the sequence regions that are simultaneously shown in bold magenta font and underlined. (a) Human Major Prion Protein. Structural information is from the PDB entry 4 KML chain A. The N-terminal residues 1–116 are not present in the structure. (b) Human Amyloid-β peptide 1–42. Structural information is from the PDB entry 2BEG, which shows this peptide in fibrillary form. N-terminal residues 1–16 are not present in the structure. (c) Human Insulin. Structural information was taken from the PDB entry 3EY7. The chains A and B are shown in yellow and blue ribbons. The disulfide bonds are also shown. (d) Human Pmel. No structural information is available for this protein.