Alpha-synuclein: Difference between revisions
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The Syn structure shows <scene name='84/840509/Cv/2'>8 β-sheet</scene> forming segments interrupted by <scene name='84/840509/Cv/4'>Gly residues</scene>. Seven PD-associated familial <scene name='84/840509/Cv/5'>mutations</scene> are known. The 3D structure shows a <scene name='84/840509/Cv/6'>hydrophobic cleft</scene> which can provide an entry point for an incoming Syn molecule elongating the fibril<ref>PMID:29969391</ref>. | The Syn structure shows <scene name='84/840509/Cv/2'>8 β-sheet</scene> forming segments interrupted by <scene name='84/840509/Cv/4'>Gly residues</scene>. Seven PD-associated familial <scene name='84/840509/Cv/5'>mutations</scene> are known. The 3D structure shows a <scene name='84/840509/Cv/6'>hydrophobic cleft</scene> which can provide an entry point for an incoming Syn molecule elongating the fibril<ref>PMID:29969391</ref>. | ||
== 3D Structures of alpha-synuclein== | == 3D Structures of alpha-synuclein== | ||
[[Alpha-synuclein 3D structures]] | |||
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== References == | == References == | ||
<references/> | <references/> | ||
</StructureSection> | |||
[[Category:Topic Page]] | [[Category:Topic Page]] |
Revision as of 11:59, 24 September 2024
FunctionAlpha-Synuclein (Syn) is a human neuronal protein which has several roles in synaptic activity. Syn enhances vesicle priming, fusion and dilation of exocytotic pores[1]. Syn acts as a molecular chaperone in assisting the folding of SNAREs - the synaptic fusion components[2]. Syn associates with the dopamine transporter and modulates its activity[3]. DiseaseSyn is a central component in the pathogenicity of Parkinson Disease (PD). PD is associated with deposition of Syn in the form of Lewy bodies throughout the brain and loss of dopaminergic neuronal cells[4]. RelevanceVarious therapeutic approaches are investigated such as blocking of Syn receptors and searching for small molecules to target Syn aggregation and increase its degradation by increasing [5]. Structural highlightsThe Syn structure shows forming segments interrupted by . Seven PD-associated familial are known. The 3D structure shows a which can provide an entry point for an incoming Syn molecule elongating the fibril[6]. 3D Structures of alpha-synucleinUpdated on 04-May-2025 6h6b, 6a6b, 6cu7, 6cu8, 6l1t, 6l1u, 6l4s, 6lrq,6rt0, 6rtb, 6sst, 6ssx, 6xyo, 6xyp, 6xyq, 6osj, 6osl, 6osm, 7c1d, 7l7h, 7nca, 7ncg, 7nch, 7nci, 7ncj, 7nck, 7ozg, 7ozh, 7v47, 7v48, 7v4a, 7v4b, 7v4c, 7v4d, 8a4l – hSyn – human - Cryo EM 2n0a – hSyn – NMR References
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