Editing Alpha-synuclein (section)

== Sequence ==

Alpha-synuclein [[primary structure]] is usually divided in three distinct domains:
* Residues 1-60: An [[amphiphile|amphipathic]] N-terminal region dominated by four 11-residue repeats including the [[consensus sequence]] KTKEGV. This sequence has a structural [[alpha helix]] propensity similar to apolipoproteins-binding domains.<ref>{{cite journal | vauthors = Clayton DF, George JM | title = The synucleins: a family of proteins involved in synaptic function, plasticity, neurodegeneration and disease | journal = Trends in Neurosciences | volume = 21 | issue = 6 | pages = 249–254 | date = June 1998 | pmid = 9641537 | doi = 10.1016/S0166-2236(97)01213-7 | s2cid = 20654921 }}</ref> It is a highly conserved terminal that interacts with acidic lipid membranes, and all the discovered point mutations of the SNCA [[gene]] are located within this terminal.<ref>{{cite journal | vauthors = Bussell R, Eliezer D | title = A structural and functional role for 11-mer repeats in alpha-synuclein and other exchangeable lipid binding proteins | journal = Journal of Molecular Biology | volume = 329 | issue = 4 | pages = 763–778 | date = June 2003 | pmid = 12787676 | doi = 10.1016/S0022-2836(03)00520-5 }}</ref>
* Residues 61-95: A central hydrophobic region which includes the ''non-amyloid-β component'' (NAC) region, involved in protein aggregation.<ref name="Ueda_1993" /> This domain is unique to alpha-synuclein among the synuclein family.<ref>{{cite journal | vauthors = Uchihara T, Giasson BI | title = Propagation of alpha-synuclein pathology: hypotheses, discoveries, and yet unresolved questions from experimental and human brain studies | journal = Acta Neuropathologica | volume = 131 | issue = 1 | pages = 49–73 | date = January 2016 | pmid = 26446103 | pmc = 4698305 | doi = 10.1007/s00401-015-1485-1 }}</ref>
* Residues 96-140: a highly acidic and [[proline]]-rich region which has no distinct structural propensity. This domain plays an important role in the function, solubility and interaction of alpha-synuclein with other [[protein]]s.<ref>{{cite journal | vauthors = Sorrentino ZA, Xia Y, Gorion KM, Hass E, Giasson BI | title = Carboxy-terminal truncations of mouse α-synuclein alter aggregation and prion-like seeding | journal = FEBS Letters | volume = 594 | issue = 8 | pages = 1271–1283 | date = April 2020 | pmid = 31912891 | pmc = 7188589 | doi = 10.1002/1873-3468.13728 }}</ref><ref name="Burre_2010" />