Alpha-synuclein: Difference between revisions
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<StructureSection load='6flt' size='340' side='right' caption='Human alpha-synuclein (PDB [[6flt]])' scene=''> | <StructureSection load='6flt' size='340' side='right' caption='Human alpha-synuclein (PDB [[6flt]])' scene='84/840509/Cv/1'> | ||
== Function == | == Function == | ||
'''Alpha-Synuclein''' (Syn) is a human neuronal protein which has several roles in synaptic activity. Syn enhances vesicle priming, fusion and dilation of exocytotic pores<ref>PMID:28288128</ref>. Syn acts as a molecular chaperone in assisting the folding of SNAREs - the synaptic fusion components<ref>PMID:20798282</ref>. | '''Alpha-Synuclein''' (Syn) is a human neuronal protein which has several roles in synaptic activity. Syn enhances vesicle priming, fusion and dilation of exocytotic pores<ref>PMID:28288128</ref>. Syn acts as a molecular chaperone in assisting the folding of SNAREs - the synaptic fusion components<ref>PMID:20798282</ref>. Syn associates with the dopamine transporter and modulates its activity<ref>PMID:26442590</ref>. | ||
== Disease == | == Disease == | ||
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== Structural highlights == | == Structural highlights == | ||
The Syn structure shows 8 β-sheet forming segments interrupted by Gly residues. Seven PD-associated familial mutations are known. | The Syn structure shows 8 β-sheet forming segments interrupted by Gly residues. Seven PD-associated familial mutations are known. The 3D structure shows a hydrophobic cleft which can provide an entry point for an incoming Syn molecule elongating the fibril<ref>PMID:29969391</ref>. | ||
</StructureSection> | </StructureSection> | ||