7xo1: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7xo1]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XO1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XO1 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7xo1]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XO1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XO1 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7xo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xo1 OCA], [https://pdbe.org/7xo1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xo1 RCSB], [https://www.ebi.ac.uk/pdbsum/7xo1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xo1 ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7xo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xo1 OCA], [https://pdbe.org/7xo1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xo1 RCSB], [https://www.ebi.ac.uk/pdbsum/7xo1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xo1 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Disease == | == Disease == | ||
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/SYUA_HUMAN SYUA_HUMAN] May be involved in the regulation of dopamine release and transport. Induces fibrillization of microtubule-associated protein tau. Reduces neuronal responsiveness to various apoptotic stimuli, leading to a decreased caspase-3 activation. | [https://www.uniprot.org/uniprot/SYUA_HUMAN SYUA_HUMAN] May be involved in the regulation of dopamine release and transport. Induces fibrillization of microtubule-associated protein tau. Reduces neuronal responsiveness to various apoptotic stimuli, leading to a decreased caspase-3 activation. | ||
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== Publication Abstract from PubMed == | |||
alpha-Synuclein (alpha-syn) has been shown to form various conformational fibrils associated with different synucleinopathies. But whether the conformation of alpha-syn fibrils changes during disease progression is unclear. Here, we amplified alpha-syn aggregates from the cerebrospinal fluid (CSF) of patients with Parkinson's disease (PD) staged in preclinical PD (pre-PD), middle- to late-stage PD (mid-PD), and late-stage PD (late-PD). Our results show that alpha-syn fibrils derived from the late-PD patient are most potent in inducing endogenous alpha-syn aggregation in primary neurons, followed by the mid-PD and pre-PD fibrils. By using cryo-electron microscopy, we further determined the high-resolution structures of the CSF-amplified fibrils. The structures exhibit remarkable differences in a minor but significant population of conformational species in different staged samples. Our work demonstrates structural and pathological differences between alpha-syn fibrils derived from PD patients at a spectrum of clinical stages, which suggests potential conformational transition of alpha-syn fibrils during the progression of PD. | |||
Conformational change of alpha-synuclein fibrils in cerebrospinal fluid from different clinical phases of Parkinson's disease.,Fan Y, Sun Y, Yu W, Tao Y, Xia W, Liu Y, Zhao Q, Tang Y, Sun Y, Liu F, Cao Q, Wu J, Liu C, Wang J, Li D Structure. 2023 Jan 5;31(1):78-87.e5. doi: 10.1016/j.str.2022.11.013. Epub 2022 , Dec 12. PMID:36513068<ref>PMID:36513068</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | == References == | ||
<references/> | <references/> | ||