5hhe - Revision history

OCA at 07:36, 9 August 2023

OCA — Wed, 09 Aug 2023 07:36:34 GMT

←Older revision		Revision as of 07:36, 9 August 2023
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	<StructureSection load='5hhe' size='340' side='right'caption='[[5hhe]], [[Resolution\|resolution]] 1.46Å' scene=''>		<StructureSection load='5hhe' size='340' side='right'caption='[[5hhe]], [[Resolution\|resolution]] 1.46Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5hhe]] is a 2 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=5HHE OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5HHE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5hhe]] is a 2 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=5HHE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HHE FirstGlance]. <br>
-	</td></tr><tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~BECN1~~, ~~GT197 (~~[~~http://www~~.~~ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info~~&~~srchmode=5&id=9606 HUMAN])~~</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]] 1.46Å</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5hhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hhe OCA], [~~http~~://pdbe.org/5hhe PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5hhe RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5hhe PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5hhe 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=5hhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hhe OCA], [https://pdbe.org/5hhe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hhe RCSB], [https://www.ebi.ac.uk/pdbsum/5hhe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hhe ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/BECN1_HUMAN BECN1_HUMAN]] Plays a central role in autophagy. Required for the abcission step in cytokinesis. May play a role in antiviral host defense. Protects against infection by a neurovirulent strain of Sindbis virus.<ref>PMID:20208530</ref>	+	[https://www.uniprot.org/uniprot/BECN1_HUMAN BECN1_HUMAN] Plays a central role in autophagy. Required for the abcission step in cytokinesis. May play a role in antiviral host defense. Protects against infection by a neurovirulent strain of Sindbis virus.<ref>PMID:20208530</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Mei, Y]]	+	[[Category: Mei Y]]
-	[[Category: Sinha, S]]	+	[[Category: Sinha S]]
-	~~[[Category: Anti-parallel dimer]]~~	+
-	~~[[Category: Autophagy regulator]]~~	+
-	~~[[Category: Cell cycle]]~~	+
-	~~[[Category: Coiled-coil domain~~]]	+

OCA at 07:05, 20 May 2020

OCA — Wed, 20 May 2020 07:05:52 GMT

←Older revision		Revision as of 07:05, 20 May 2020
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	==Human Beclin 1 coiled-coil domain==		==Human Beclin 1 coiled-coil domain==
-	<StructureSection load='5hhe' size='340' side='right' caption='[[5hhe]], [[Resolution\|resolution]] 1.46Å' scene=''>	+	<StructureSection load='5hhe' size='340' side='right'caption='[[5hhe]], [[Resolution\|resolution]] 1.46Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5hhe]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HHE OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5HHE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5hhe]] is a 2 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=5HHE OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5HHE FirstGlance]. <br>
-	</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=5hhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hhe OCA], [http://pdbe.org/5hhe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hhe RCSB], [http://www.ebi.ac.uk/pdbsum/5hhe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hhe ProSAT]</span></td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BECN1, GT197 ([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://proteopedia.org/fgij/fg.htm?mol=5hhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hhe OCA], [http://pdbe.org/5hhe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hhe RCSB], [http://www.ebi.ac.uk/pdbsum/5hhe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hhe ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Mei, Y]]		[[Category: Mei, Y]]
	[[Category: Sinha, S]]		[[Category: Sinha, S]]

OCA at 08:09, 27 July 2016

OCA — Wed, 27 Jul 2016 08:09:08 GMT

←Older revision		Revision as of 08:09, 27 July 2016
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	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/BECN1_HUMAN BECN1_HUMAN]] Plays a central role in autophagy. Required for the abcission step in cytokinesis. May play a role in antiviral host defense. Protects against infection by a neurovirulent strain of Sindbis virus.<ref>PMID:20208530</ref>		[[http://www.uniprot.org/uniprot/BECN1_HUMAN BECN1_HUMAN]] Plays a central role in autophagy. Required for the abcission step in cytokinesis. May play a role in antiviral host defense. Protects against infection by a neurovirulent strain of Sindbis virus.<ref>PMID:20208530</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Autophagy, an essential eukaryotic homeostasis pathway, allows the sequestration of unwanted, damaged, or harmful cytoplasmic components in vesicles called autophagosomes, permitting subsequent lysosomal degradation and nutrient recycling. Autophagosome nucleation is mediated by class III phosphatidylinositol-3-kinase complexes that include two key autophagy proteins, BECN1/Beclin 1 and ATG14/BARKOR, which form parallel heterodimers via their coiled-coil domains (CCDs). Here we present the 1.46 A X-ray crystal structure of the antiparallel, human BECN1 CCD homodimer, which represents BECN1 oligomerization outside the autophagosome nucleation complex. We use circular dichroism and small-angle X-ray scattering (SAXS) to show that the ATG14 CCD is significantly disordered but becomes more helical in the BECN1:ATG14 heterodimer, although it is less well-folded than the BECN1 CCD homodimer. SAXS also indicates that the BECN1:ATG14 heterodimer is more curved than other BECN1-containing CCD dimers, which has important implications for the structure of the autophagosome nucleation complex. A model of the BECN1:ATG14 CCD heterodimer that agrees well with the SAXS data shows that BECN1 residues at the homodimer interface are also responsible for heterodimerization, allowing us to identify ATG14 interface residues. Finally, we verify the role of BECN1 and ATG14 interface residues in binding by assessing the impact of point mutations of these residues on co-immunoprecipitation of the partner and demonstrate that these mutations abrogate starvation-induced upregulation of autophagy but do not impact basal autophagy. Thus, this research provides insights into structures of the BECN1 CCD homodimer and the BECN1:ATG14 CCD heterodimer and identifies interface residues that are important for BECN1:ATG14 heterodimerization and for autophagy.
		+
		+	Identification of BECN1 and ATG14 Coiled-Coil Interface Residues That Are Important for Starvation-Induced Autophagy.,Mei Y, Su M, Sanishvili R, Chakravarthy S, Colbert CL, Sinha SC Biochemistry. 2016 Jul 22. PMID:27383850<ref>PMID:27383850</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5hhe" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 15:34, 26 July 2016

OCA — Tue, 26 Jul 2016 15:34:08 GMT

←Older revision		Revision as of 15:34, 26 July 2016
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-	'''Unreleased structure'''

-	~~The entry~~ 5hhe ~~is ON HOLD until Paper Publication~~	+	==Human Beclin 1 coiled-coil domain==
-		+	<StructureSection load='5hhe' size='340' side='right' caption='[[5hhe]], [[Resolution\|resolution]] 1.46Å' scene=''>
-	~~Authors~~: ~~Mei~~, Y., ~~Sinha~~, S.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5hhe]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HHE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HHE FirstGlance]. <br>
-	~~Description~~: ~~Human Beclin 1 coiled~~-~~coil domain~~	+	</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=5hhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hhe OCA], [http://pdbe.org/5hhe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hhe RCSB], [http://www.ebi.ac.uk/pdbsum/5hhe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hhe ProSAT]</span></td></tr>
-	[[~~Category~~: ~~Unreleased Structures~~]]	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/BECN1_HUMAN BECN1_HUMAN]] Plays a central role in autophagy. Required for the abcission step in cytokinesis. May play a role in antiviral host defense. Protects against infection by a neurovirulent strain of Sindbis virus.<ref>PMID:20208530</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Mei, Y]]		[[Category: Mei, Y]]
	[[Category: Sinha, S]]		[[Category: Sinha, S]]
		+	[[Category: Anti-parallel dimer]]
		+	[[Category: Autophagy regulator]]
		+	[[Category: Cell cycle]]
		+	[[Category: Coiled-coil domain]]

OCA at 00:41, 28 January 2016

OCA — Thu, 28 Jan 2016 00:41:12 GMT

←Older revision		Revision as of 00:41, 28 January 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5hhe is ON HOLD	+	The entry 5hhe is ON HOLD until Paper Publication

	Authors: Mei, Y., Sinha, S.		Authors: Mei, Y., Sinha, S.

OCA: Protected "5hhe" [edit=sysop:move=sysop]

OCA — Wed, 20 Jan 2016 15:26:34 GMT

Protected "5hhe" [edit=sysop:move=sysop]

←Older revision

Revision as of 15:26, 20 January 2016

OCA: New page: '''Unreleased structure''' The entry 5hhe is ON HOLD Authors: Mei, Y., Sinha, S. Description: Human Beclin 1 coiled-coil domain Category: Unreleased Structures Category: Mei, Y...

OCA — Wed, 20 Jan 2016 15:26:32 GMT

New page: '''Unreleased structure''' The entry 5hhe is ON HOLD Authors: Mei, Y., Sinha, S. Description: Human Beclin 1 coiled-coil domain Category: Unreleased Structures Category: Mei, Y...

New page

'''Unreleased structure'''

The entry 5hhe is ON HOLD

Authors: Mei, Y., Sinha, S.

Description: Human Beclin 1 coiled-coil domain
[[Category: Unreleased Structures]]
[[Category: Mei, Y]]
[[Category: Sinha, S]]