Residues 61-95: A central hydrophobic region which includes the non-amyloid-β component (NAC) region, involved in protein aggregation This sequence has a structural alpha helix propensity similar to apolipoproteins-binding domains Residues 1-60: An amphipathic N-terminal region dominated by four 11-residue repeats including the consensus sequence KTKEGV. The release of neurotransmitters relays signals between neurons and is critical for normal brain function.Alpha-synuclein primary structure is usually divided in three distinct domains: Presynaptic terminals release chemical messengers, called neurotransmitters, from compartments known as synaptic vesicles. Within these structures, alpha-synuclein interacts with phospholipids and proteins.
Hence certain mutations of alpha-synuclein may cause it to form amyloid-like fibrils that contribute to Parkinson's disease.-One of the polypeptide chains making up the 4 0Structure of hemoglobin S undergoes a mutation.- Glutamic Acid (Polar) to Valine (Nonpolar, Hydrophobic)-Abnormal hydrophobic patch on the surface of the polypeptide. Genomic duplication and triplication of the gene appear to be a rare cause of Parkinson's disease in other lineages, although more common than point mutations. Three point mutations have been identified thus far: A53T, A30P and E46K.
0 kommentar(er)
