3q29: Difference between revisions
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==Cyrstal structure of human alpha-synuclein (1-19) fused to maltose binding protein (MBP)== | |||
<StructureSection load='3q29' size='340' side='right' caption='[[3q29]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3q29]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q29 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3Q29 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAL:MALTOSE'>MAL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3q25|3q25]], [[3q26|3q26]], [[3q27|3q27]], [[3q28|3q28]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SNCA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3q29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q29 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3q29 RCSB], [http://www.ebi.ac.uk/pdbsum/3q29 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Aggregates of the protein alpha-synuclein are the main component of Lewy bodies, the hallmark of Parkinson's disease. alpha-Synuclein aggregates are also found in many human neurodegenerative diseases known as synucleinopathies. In vivo, alpha-synuclein associates with membranes and adopts alpha-helical conformations. The details of how alpha-synuclein converts from the functional native state to amyloid aggregates remain unknown. In this study, we use maltose-binding protein (MBP) as a carrier to crystallize segments of alpha-synuclein. From crystal structures of fusions between MBP and four segments of alpha-synuclein, we have been able to trace a virtual model of the first 72 residues of alpha-synuclein. Instead of a mostly alpha-helical conformation observed in the lipid environment, our crystal structures show alpha-helices only at residues 1-13 and 20-34. The remaining segments are extended loops or coils. All of the predicted fiber-forming segments based on the 3D profile method are in extended conformations. We further show that the MBP fusion proteins with fiber-forming segments from alpha-synuclein can also form fiber-like nano-crystals or amyloid-like fibrils. Our structures suggest intermediate states during amyloid formation of alpha-synuclein. | |||
Structures of segments of alpha-synuclein fused to maltose-binding protein suggest intermediate states during amyloid formation.,Zhao M, Cascio D, Sawaya MR, Eisenberg D Protein Sci. 2011 Jun;20(6):996-1004. doi: 10.1002/pro.630. Epub 2011 May, 3. PMID:21462277<ref>PMID:21462277</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Cascio, D | [[Category: Cascio, D]] | ||
[[Category: Eisenberg, D | [[Category: Eisenberg, D]] | ||
[[Category: Sawaya, M R | [[Category: Sawaya, M R]] | ||
[[Category: Zhao, M | [[Category: Zhao, M]] | ||
[[Category: Amyloid]] | [[Category: Amyloid]] | ||
[[Category: Fusion protein]] | [[Category: Fusion protein]] | ||
[[Category: Protein fibril]] | [[Category: Protein fibril]] | ||
[[Category: Sugar binding protein]] | [[Category: Sugar binding protein]] | ||
Revision as of 13:14, 19 December 2014
Cyrstal structure of human alpha-synuclein (1-19) fused to maltose binding protein (MBP)Cyrstal structure of human alpha-synuclein (1-19) fused to maltose binding protein (MBP)
Structural highlights
Publication Abstract from PubMedAggregates of the protein alpha-synuclein are the main component of Lewy bodies, the hallmark of Parkinson's disease. alpha-Synuclein aggregates are also found in many human neurodegenerative diseases known as synucleinopathies. In vivo, alpha-synuclein associates with membranes and adopts alpha-helical conformations. The details of how alpha-synuclein converts from the functional native state to amyloid aggregates remain unknown. In this study, we use maltose-binding protein (MBP) as a carrier to crystallize segments of alpha-synuclein. From crystal structures of fusions between MBP and four segments of alpha-synuclein, we have been able to trace a virtual model of the first 72 residues of alpha-synuclein. Instead of a mostly alpha-helical conformation observed in the lipid environment, our crystal structures show alpha-helices only at residues 1-13 and 20-34. The remaining segments are extended loops or coils. All of the predicted fiber-forming segments based on the 3D profile method are in extended conformations. We further show that the MBP fusion proteins with fiber-forming segments from alpha-synuclein can also form fiber-like nano-crystals or amyloid-like fibrils. Our structures suggest intermediate states during amyloid formation of alpha-synuclein. Structures of segments of alpha-synuclein fused to maltose-binding protein suggest intermediate states during amyloid formation.,Zhao M, Cascio D, Sawaya MR, Eisenberg D Protein Sci. 2011 Jun;20(6):996-1004. doi: 10.1002/pro.630. Epub 2011 May, 3. PMID:21462277[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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