Alpha-synuclein
From Proteopedia
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(New page: <StructureSection load='6flt' size='340' side='right' caption='Human alpha-synuclein (PDB 6flt)' scene=''> == Function == '''Alpha-Synuclein''' (Syn) is a human neuronal protein whi...) |
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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=''> | ||
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== Structural highlights == | == Structural highlights == | ||
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| + | 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> | ||
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[[3q25]], [[3q26]], [[3q27]], [[3q28]], [[3q29]] – hSyn peptide/MBP<br /> | [[3q25]], [[3q26]], [[3q27]], [[3q28]], [[3q29]] – hSyn peptide/MBP<br /> | ||
[[3q26]] – hSyn residues 10-42/MBP<br /> | [[3q26]] – hSyn residues 10-42/MBP<br /> | ||
| + | [[4r0u]], [[4r0w]], [[4rik]], [[4ril]] - hSyn amyloid-forming peptide<br /> | ||
| + | [[4znn]] - hSyn amyloid-forming peptide (mutant)<br /> | ||
== References == | == References == | ||
Revision as of 09:11, 4 April 2020
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3D Structures of alpha-synuclein
Updated on 04-April-2020
6flt, 6h6b, 6a6b, 6cu7, 6cu8, 6rt0, 6rtb, 6sst, 6ssx, 6xyo, 6xyp, 6xyq, 6osj, 6osl, 6osm – hSyn – human - Cryo EM
2n0a – hSyn – NMR
6ufr, 6peo, 6pes – hSyn (mutant) - Cryo EM
2m55 – hSyn residues 1-19 + calmodulin – NMR
6i42 – hSyn residues 48-60 + cyclophilin A
5crw – hSyn residues 31-41 + protein disulfide isomerase
6ct7 – hSyn residues 1-10 + antibody
2x6m – hSyn residues 132-140 + antibody
3q25, 3q26, 3q27, 3q28, 3q29 – hSyn peptide/MBP
3q26 – hSyn residues 10-42/MBP
4r0u, 4r0w, 4rik, 4ril - hSyn amyloid-forming peptide
4znn - hSyn amyloid-forming peptide (mutant)
References
- ↑ PMID:28288128/ref>. Syn acts as a molecular chaperone in assisting the folding of SNAREs - the synaptic fusion components<ref>PMID:20798282</li> <li id="cite_note-1">[[#cite_ref-1|↑]] Butler B, Saha K, Rana T, Becker JP, Sambo D, Davari P, Goodwin JS, Khoshbouei H. Dopamine Transporter Activity Is Modulated by alpha-Synuclein. J Biol Chem. 2015 Dec 4;290(49):29542-54. doi: 10.1074/jbc.M115.691592. Epub 2015, Oct 6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/26442590 26442590] doi:[http://dx.doi.org/10.1074/jbc.M115.691592 http://dx.doi.org/10.1074/jbc.M115.691592]</li> <li id="cite_note-2">[[#cite_ref-2|↑]] Xu L, Pu J. Alpha-Synuclein in Parkinson's Disease: From Pathogenetic Dysfunction to Potential Clinical Application. Parkinsons Dis. 2016;2016:1720621. doi: 10.1155/2016/1720621. Epub 2016 Aug 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/27610264 27610264] doi:[http://dx.doi.org/10.1155/2016/1720621 http://dx.doi.org/10.1155/2016/1720621]</li> <li id="cite_note-3">[[#cite_ref-3|↑]] Fields CR, Bengoa-Vergniory N, Wade-Martins R. Targeting Alpha-Synuclein as a Therapy for Parkinson's Disease. Front Mol Neurosci. 2019 Dec 5;12:299. doi: 10.3389/fnmol.2019.00299. eCollection, 2019. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/31866823 31866823] doi:[http://dx.doi.org/10.3389/fnmol.2019.00299 http://dx.doi.org/10.3389/fnmol.2019.00299]</li> <li id="cite_note-4">[[#cite_ref-4|↑]] Guerrero-Ferreira R, Taylor NMI, Mona D, Ringler P, Lauer ME, Riek R, Britschgi M, Stahlberg H. Cryo-EM structure of alpha-synuclein fibrils. Elife. 2018 Jul 3;7. pii: 36402. doi: 10.7554/eLife.36402. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/29969391 29969391] doi:[http://dx.doi.org/10.7554/eLife.36402 http://dx.doi.org/10.7554/eLife.36402]</li></ol></ref>
