3q27 - Revision history

OCA at 11:30, 14 March 2024

2024-03-14T11:30:32Z

←Older revision		Revision as of 11:30, 14 March 2024
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	<StructureSection load='3q27' size='340' side='right'caption='[[3q27]], [[Resolution\|resolution]] 1.30Å' scene=''>		<StructureSection load='3q27' size='340' side='right'caption='[[3q27]], [[Resolution\|resolution]] 1.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3q27]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q27 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q27 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3q27]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q27 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q27 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=GLC:ALPHA~~-~~D-GLUCOSE'>GLC</scene>~~, ~~<scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.302Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max~~-~~height: 3em;~~'>~~[[3q25\|3q25]], [[3q26\|3q26]], [[3q28\|3q28]], [[3q29\|3q29]]~~</~~div~~><~~/td~~></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<~~tr id~~='~~gene~~'><~~td class="sblockLbl"~~><~~b>[[Gene\|Gene~~:~~]]</b~~></td>~~<td class="sblockDat">SNCA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])~~</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=3q27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q27 OCA], [https://pdbe.org/3q27 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q27 RCSB], [https://www.ebi.ac.uk/pdbsum/3q27 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q27 ProSAT]</span></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=3q27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q27 OCA], [https://pdbe.org/3q27 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q27 RCSB], [https://www.ebi.ac.uk/pdbsum/3q27 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q27 ProSAT]</span></td></tr>
	</table>		</table>
		+	== Disease ==
		+	[https://www.uniprot.org/uniprot/SYUA_HUMAN SYUA_HUMAN] Note=Genetic alterations of SNCA resulting in aberrant polymerization into fibrils, are associated with several neurodegenerative diseases (synucleinopathies). SNCA fibrillar aggregates represent the major non A-beta component of Alzheimer disease amyloid plaque, and a major component of Lewy body inclusions. They are also found within Lewy body (LB)-like intraneuronal inclusions, glial inclusions and axonal spheroids in neurodegeneration with brain iron accumulation type 1. Defects in SNCA are the cause of Parkinson disease type 1 (PARK1) [MIM:[https://omim.org/entry/168601 168601]. A complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability. Additional features are characteristic postural abnormalities, dysautonomia, dystonic cramps, and dementia. The pathology of Parkinson disease involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. The disease is progressive and usually manifests after the age of 50 years, although early-onset cases (before 50 years) are known. The majority of the cases are sporadic suggesting a multifactorial etiology based on environmental and genetic factors. However, some patients present with a positive family history for the disease. Familial forms of the disease usually begin at earlier ages and are associated with atypical clinical features.<ref>PMID:9197268</ref> <ref>PMID:9462735</ref> <ref>PMID:14755719</ref> Defects in SNCA are the cause of Parkinson disease type 4 (PARK4) [MIM:[https://omim.org/entry/605543 605543]. A complex neurodegenerative disorder with manifestations ranging from typical Parkinson disease to dementia with Lewy bodies. Clinical features include parkinsonian symptoms (tremor, rigidity, postural instability and bradykinesia), dementia, diffuse Lewy body pathology, autonomic dysfunction, hallucinations and paranoia. Defects in SNCA are the cause of dementia Lewy body (DLB) [MIM:[https://omim.org/entry/127750 127750]. A neurodegenerative disorder clinically characterized by mental impairment leading to dementia, parkinsonism, often with fluctuating cognitive function, visual hallucinations, falls, syncopal episodes, and sensitivity to neuroleptic medication. Brainstem or cortical intraneuronal accumulations of aggregated proteins (Lewy bodies) are the only essential pathologic features. Patients may also have hippocampal and neocortical senile plaques, sometimes in sufficient number to fulfill the diagnostic criteria for Alzheimer disease.
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI]] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.	+	[https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.[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.
-	~~<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>~~	+
-	~~<div class="pdbe-citations 3q27" style="background-color:#fffaf0;"></div>~~	+

	==See Also==		==See Also==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Escherichia coli]]
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Cascio, D]]	+	[[Category: Cascio D]]
-	[[Category: Eisenberg, D]]	+	[[Category: Eisenberg D]]
-	[[Category: Sawaya~~, M R~~]]	+	[[Category: Sawaya MR]]
-	[[Category: Zhao, M]]	+	[[Category: Zhao M]]
-	~~[[Category: Amyloid]]~~	+
-	~~[[Category: Fusion protein]]~~	+
-	~~[[Category: Protein fibril]]~~	+
-	~~[[Category: Sugar binding protein~~]]	+

OCA at 05:48, 8 June 2022

2022-06-08T05:48:43Z

←Older revision		Revision as of 05:48, 8 June 2022
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	==Cyrstal structure of human alpha-synuclein (32-57) fused to maltose binding protein (MBP)==		==Cyrstal structure of human alpha-synuclein (32-57) fused to maltose binding protein (MBP)==
-	<StructureSection load='3q27' size='340' side='right' caption='[[3q27]], [[Resolution\|resolution]] 1.30Å' scene=''>	+	<StructureSection load='3q27' size='340' side='right'caption='[[3q27]], [[Resolution\|resolution]] 1.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3q27]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q27 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3Q27 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3q27]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q27 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q27 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>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]], [[3q28\|3q28]], [[3q29\|3q29]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3q25\|3q25]], [[3q26\|3q26]], [[3q28\|3q28]], [[3q29\|3q29]]</div></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=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SNCA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3q27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q27 OCA], [~~http~~://pdbe.org/3q27 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3q27 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3q27 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3q27 ProSAT]</span></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=3q27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q27 OCA], [https://pdbe.org/3q27 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q27 RCSB], [https://www.ebi.ac.uk/pdbsum/3q27 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q27 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI]] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.	+	[[https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI]] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</div>		</div>
	<div class="pdbe-citations 3q27" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3q27" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Alpha-synuclein\|Alpha-synuclein]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Cascio, D]]		[[Category: Cascio, D]]
	[[Category: Eisenberg, D]]		[[Category: Eisenberg, D]]

OCA at 13:24, 5 August 2016

2016-08-05T13:24:24Z

←Older revision		Revision as of 13:24, 5 August 2016
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		+
	==Cyrstal structure of human alpha-synuclein (32-57) fused to maltose binding protein (MBP)==		==Cyrstal structure of human alpha-synuclein (32-57) fused to maltose binding protein (MBP)==
	<StructureSection load='3q27' size='340' side='right' caption='[[3q27]], [[Resolution\|resolution]] 1.30Å' scene=''>		<StructureSection load='3q27' size='340' side='right' caption='[[3q27]], [[Resolution\|resolution]] 1.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3q27]] is a 1 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=3Q27 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3Q27 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3q27]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q27 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3Q27 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>		</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]], [[3q28\|3q28]], [[3q29\|3q29]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3q25\|3q25]], [[3q26\|3q26]], [[3q28\|3q28]], [[3q29\|3q29]]</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='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=9606 HUMAN])</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=3q27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q27 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3q27 RCSB], [http://www.ebi.ac.uk/pdbsum/3q27 PDBsum]</span></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=3q27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q27 OCA], [http://pdbe.org/3q27 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3q27 RCSB], [http://www.ebi.ac.uk/pdbsum/3q27 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3q27 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 3q27" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Escherichia coli~~]]	+	[[Category: Human]]
	[[Category: Cascio, D]]		[[Category: Cascio, D]]
	[[Category: Eisenberg, D]]		[[Category: Eisenberg, D]]

OCA at 19:11, 25 December 2014

2014-12-25T19:11:08Z

←Older revision		Revision as of 19:11, 25 December 2014
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	<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=3q27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q27 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3q27 RCSB], [http://www.ebi.ac.uk/pdbsum/3q27 PDBsum]</span></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=3q27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q27 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3q27 RCSB], [http://www.ebi.ac.uk/pdbsum/3q27 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI]] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 10:29, 19 December 2014

2014-12-19T10:29:53Z

←Older revision		Revision as of 10:29, 19 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3q27\| PDB=3q27 \| SCENE= }}~~	+	==Cyrstal structure of human alpha-synuclein (32-57) fused to maltose binding protein (MBP)==
-	===Cyrstal structure of human alpha-synuclein (32-57) fused to maltose binding protein (MBP)===	+	<StructureSection load='3q27' size='340' side='right' caption='[[3q27]], [[Resolution\|resolution]] 1.30Å' scene=''>
-	~~{{ABSTRACT_PUBMED_21462277}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3q27]] is a 1 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=3Q27 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3Q27 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]], [[3q28\|3q28]], [[3q29\|3q29]]</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=3q27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q27 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3q27 RCSB], [http://www.ebi.ac.uk/pdbsum/3q27 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.

-	~~==Function==~~	+	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>
-	~~[[http~~:~~//www~~.~~uniprot~~.~~org~~/~~uniprot/MALE_ECOLI MALE_ECOLI]] Involved in the high-affinity maltose membrane transport system MalEFGK~~. ~~Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides~~.	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[3q27]] is~~ a ~~1 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=3Q27 OCA].~~	+	</div>
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:021462277</ref>~~<references ~~group="xtra"~~/><~~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]]

OCA at 23:05, 24 March 2013

2013-03-24T23:05:06Z

←Older revision		Revision as of 23:05, 24 March 2013
Line 1:		Line 1:
-	[[Image:3q27.jpg\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_3q27", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_3q27\| PDB=3q27 \| SCENE= }}		{{STRUCTURE_3q27\| PDB=3q27 \| SCENE= }}
-
	===Cyrstal structure of human alpha-synuclein (32-57) fused to maltose binding protein (MBP)===		===Cyrstal structure of human alpha-synuclein (32-57) fused to maltose binding protein (MBP)===
		+	{{ABSTRACT_PUBMED_21462277}}

-		+	==Function==
-	~~<!--~~	+	[[http://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI]] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_21462277}}, adds the Publication Abstract to the page~~	+
-	~~(as it appears on PubMed at~~ http://www.~~pubmed~~.~~gov), where 21462277 is~~ the ~~PubMed ID number~~.	+
-	~~-->~~	+
-	~~{{ABSTRACT_PUBMED_21462277}}~~	+

	==About this Structure==		==About this Structure==
-	[[3q27]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli~~,_homo_sapiens~~ Escherichia coli~~, homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q27 OCA].	+	[[3q27]] is a 1 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=3Q27 OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:021462277</ref><references group="xtra"/>	+	<ref group="xtra">PMID:021462277</ref><references group="xtra"/><references/>
-	[[Category: Escherichia coli~~, homo sapiens~~]]	+	[[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: Fusion protein]]
		+	[[Category: Protein fibril]]
		+	[[Category: Sugar binding protein]]

OCA at 05:44, 1 June 2011

2011-06-01T05:44:06Z

←Older revision		Revision as of 05:44, 1 June 2011
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3q27.jpg\|left\|200px]]

-	The ~~entry 3q27~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3q27", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3q27\| PDB=3q27 \| SCENE= }}

-	~~Authors: Zhao, M., Sawaya, M.R., Cascio, D., Eisenberg, D.~~	+	===Cyrstal structure of human alpha-synuclein (32-57) fused to maltose binding protein (MBP)===

-	~~Description: Cyrstal structure of human alpha~~-~~synuclein (32~~-~~57) fused~~ to ~~maltose binding protein~~ (~~MBP~~)	+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_21462277}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 21462277 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_21462277}}
		+
		+	==About this Structure==
		+	[[3q27]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli,_homo_sapiens Escherichia coli, homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q27 OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:021462277</ref><references group="xtra"/>
		+	[[Category: Escherichia coli, homo sapiens]]
		+	[[Category: Cascio, D.]]
		+	[[Category: Eisenberg, D.]]
		+	[[Category: Sawaya, M R.]]
		+	[[Category: Zhao, M.]]

OCA at 05:18, 16 February 2011

2011-02-16T05:18:55Z

←Older revision		Revision as of 05:18, 16 February 2011
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3q27 is ON HOLD	+	The entry 3q27 is ON HOLD until Paper Publication

	Authors: Zhao, M., Sawaya, M.R., Cascio, D., Eisenberg, D.		Authors: Zhao, M., Sawaya, M.R., Cascio, D., Eisenberg, D.

	Description: Cyrstal structure of human alpha-synuclein (32-57) fused to maltose binding protein (MBP)		Description: Cyrstal structure of human alpha-synuclein (32-57) fused to maltose binding protein (MBP)

OCA at 12:43, 26 January 2011

2011-01-26T12:43:53Z

←Older revision		Revision as of 12:43, 26 January 2011
Line 3:		Line 3:
	The entry 3q27 is ON HOLD		The entry 3q27 is ON HOLD

-	Authors: Zhao, ~~Minglei~~, Sawaya, ~~Michael~~ R., Cascio, ~~Duilio~~, Eisenberg, ~~David~~	+	Authors: Zhao, M., Sawaya, M.R., Cascio, D., Eisenberg, D.

	Description: Cyrstal structure of human alpha-synuclein (32-57) fused to maltose binding protein (MBP)		Description: Cyrstal structure of human alpha-synuclein (32-57) fused to maltose binding protein (MBP)

OCA: Protected "3q27" [edit=sysop:move=sysop]

2010-12-29T18:17:16Z

Protected "3q27" [edit=sysop:move=sysop]

←Older revision

Revision as of 18:17, 29 December 2010