1y32 - Revision history

OCA at 09:30, 6 December 2023

2023-12-06T09:30:26Z

←Older revision		Revision as of 09:30, 6 December 2023
Line 1:		Line 1:

	==NMR structure of humanin in 30% TFE solution==		==NMR structure of humanin in 30% TFE solution==
-	<StructureSection load='1y32' size='340' side='right'caption='[[1y32~~]], [[NMR_Ensembles_of_Models \| 14 NMR models~~]]' scene=''>	+	<StructureSection load='1y32' size='340' side='right'caption='[[1y32]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1y32]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y32 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1y32]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y32 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=1y32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y32 OCA], [https://pdbe.org/1y32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y32 RCSB], [https://www.ebi.ac.uk/pdbsum/1y32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y32 ProSAT]</span></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1y32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y32 OCA], [https://pdbe.org/1y32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y32 RCSB], [https://www.ebi.ac.uk/pdbsum/1y32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y32 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/HUNIN_HUMAN HUNIN_HUMAN]] Plays a role as a neuroprotective factor. Protects against death induced by multiple different familial Alzheimer disease genes and beta amyloid proteins in Alzheimer disease. Suppresses apoptosis by binding to BAX and preventing the translocation of BAX from the cytosol to mitochondria. Binds to IGFBP3 and specifically blocks IGFBP3-induced cell death Induces chemotaxis of mononuclear phagocytes via FPR2. Reduces the aggregation and fibrillary formation by suppressing the effect of APP on mononuclear phagocytes and acts by competitively inhibiting the access of FPRL1 to APP.<ref>PMID:11371646</ref> <ref>PMID:14561895</ref> <ref>PMID:11717357</ref> <ref>PMID:12732850</ref> <ref>PMID:15153530</ref>	+	[https://www.uniprot.org/uniprot/HUNIN_HUMAN HUNIN_HUMAN] Plays a role as a neuroprotective factor. Protects against death induced by multiple different familial Alzheimer disease genes and beta amyloid proteins in Alzheimer disease. Suppresses apoptosis by binding to BAX and preventing the translocation of BAX from the cytosol to mitochondria. Binds to IGFBP3 and specifically blocks IGFBP3-induced cell death Induces chemotaxis of mononuclear phagocytes via FPR2. Reduces the aggregation and fibrillary formation by suppressing the effect of APP on mononuclear phagocytes and acts by competitively inhibiting the access of FPRL1 to APP.<ref>PMID:11371646</ref> <ref>PMID:14561895</ref> <ref>PMID:11717357</ref> <ref>PMID:12732850</ref> <ref>PMID:15153530</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Benaki, D]]	+	[[Category: Benaki D]]
-	[[Category: Evangelou, A]]	+	[[Category: Evangelou A]]
-	[[Category: Livaniou, E]]	+	[[Category: Livaniou E]]
-	[[Category: Mikros, E]]	+	[[Category: Mikros E]]
-	[[Category: Pelecanou, M]]	+	[[Category: Pelecanou M]]
-	[[Category: Vlassi, M]]	+	[[Category: Vlassi M]]
-	[[Category: Zikos, C]]	+	[[Category: Zikos C]]
-	~~[[Category: Alzheimer's disease]]~~	+
-	~~[[Category: Humanin]]~~	+
-	~~[[Category: Neuroprotection]]~~	+
-	~~[[Category: Nmr solution structure]]~~	+
-	~~[[Category: Unknown function~~]]	+

OCA at 16:23, 3 November 2021

2021-11-03T16:23:09Z

←Older revision		Revision as of 16:23, 3 November 2021
Line 3:		Line 3:
	<StructureSection load='1y32' size='340' side='right'caption='[[1y32]], [[NMR_Ensembles_of_Models \| 14 NMR models]]' scene=''>		<StructureSection load='1y32' size='340' side='right'caption='[[1y32]], [[NMR_Ensembles_of_Models \| 14 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1y32]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y32 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1Y32 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1y32]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y32 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=1y32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y32 OCA], [~~http~~://pdbe.org/1y32 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1y32 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1y32 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1y32 ProSAT]</span></td></tr>	+	</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=1y32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y32 OCA], [https://pdbe.org/1y32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y32 RCSB], [https://www.ebi.ac.uk/pdbsum/1y32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y32 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/HUNIN_HUMAN HUNIN_HUMAN]] Plays a role as a neuroprotective factor. Protects against death induced by multiple different familial Alzheimer disease genes and beta amyloid proteins in Alzheimer disease. Suppresses apoptosis by binding to BAX and preventing the translocation of BAX from the cytosol to mitochondria. Binds to IGFBP3 and specifically blocks IGFBP3-induced cell death Induces chemotaxis of mononuclear phagocytes via FPR2. Reduces the aggregation and fibrillary formation by suppressing the effect of APP on mononuclear phagocytes and acts by competitively inhibiting the access of FPRL1 to APP.<ref>PMID:11371646</ref> <ref>PMID:14561895</ref> <ref>PMID:11717357</ref> <ref>PMID:12732850</ref> <ref>PMID:15153530</ref>	+	[[https://www.uniprot.org/uniprot/HUNIN_HUMAN HUNIN_HUMAN]] Plays a role as a neuroprotective factor. Protects against death induced by multiple different familial Alzheimer disease genes and beta amyloid proteins in Alzheimer disease. Suppresses apoptosis by binding to BAX and preventing the translocation of BAX from the cytosol to mitochondria. Binds to IGFBP3 and specifically blocks IGFBP3-induced cell death Induces chemotaxis of mononuclear phagocytes via FPR2. Reduces the aggregation and fibrillary formation by suppressing the effect of APP on mononuclear phagocytes and acts by competitively inhibiting the access of FPRL1 to APP.<ref>PMID:11371646</ref> <ref>PMID:14561895</ref> <ref>PMID:11717357</ref> <ref>PMID:12732850</ref> <ref>PMID:15153530</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 17:20, 29 January 2020

2020-01-29T17:20:15Z

←Older revision		Revision as of 17:20, 29 January 2020
Line 1:		Line 1:

	==NMR structure of humanin in 30% TFE solution==		==NMR structure of humanin in 30% TFE solution==
-	<StructureSection load='1y32' size='340' side='right' caption='[[1y32]], [[NMR_Ensembles_of_Models \| 14 NMR models]]' scene=''>	+	<StructureSection load='1y32' size='340' side='right'caption='[[1y32]], [[NMR_Ensembles_of_Models \| 14 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1y32]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y32 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Y32 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1y32]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y32 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Y32 FirstGlance]. <br>
Line 21:		Line 21:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Benaki, D]]		[[Category: Benaki, D]]
	[[Category: Evangelou, A]]		[[Category: Evangelou, A]]

OCA at 07:33, 18 April 2018

2018-04-18T07:33:22Z

←Older revision		Revision as of 07:33, 18 April 2018
Line 1:		Line 1:
		+
	==NMR structure of humanin in 30% TFE solution==		==NMR structure of humanin in 30% TFE solution==
	<StructureSection load='1y32' size='340' side='right' caption='[[1y32]], [[NMR_Ensembles_of_Models \| 14 NMR models]]' scene=''>		<StructureSection load='1y32' size='340' side='right' caption='[[1y32]], [[NMR_Ensembles_of_Models \| 14 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1y32]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y32 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Y32 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1y32]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y32 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Y32 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=1y32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y32 OCA], [http://pdbe.org/1y32 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y32 RCSB], [http://www.ebi.ac.uk/pdbsum/1y32 PDBsum]</span></td></tr>	+	</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=1y32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y32 OCA], [http://pdbe.org/1y32 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y32 RCSB], [http://www.ebi.ac.uk/pdbsum/1y32 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1y32 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 15:15, 10 September 2015

2015-09-10T15:15:45Z

←Older revision		Revision as of 15:15, 10 September 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1y32]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y32 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Y32 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1y32]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y32 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Y32 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=1y32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y32 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1y32 RCSB], [http://www.ebi.ac.uk/pdbsum/1y32 PDBsum]</span></td></tr>	+	</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=1y32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y32 OCA], [http://pdbe.org/1y32 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y32 RCSB], [http://www.ebi.ac.uk/pdbsum/1y32 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 15:		Line 15:
	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 1y32" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 02:03, 25 December 2014

2014-12-25T02:03:20Z

←Older revision		Revision as of 02:03, 25 December 2014
Line 5:		Line 5:
	</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=1y32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y32 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1y32 RCSB], [http://www.ebi.ac.uk/pdbsum/1y32 PDBsum]</span></td></tr>		</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=1y32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y32 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1y32 RCSB], [http://www.ebi.ac.uk/pdbsum/1y32 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/HUNIN_HUMAN HUNIN_HUMAN]] Plays a role as a neuroprotective factor. Protects against death induced by multiple different familial Alzheimer disease genes and beta amyloid proteins in Alzheimer disease. Suppresses apoptosis by binding to BAX and preventing the translocation of BAX from the cytosol to mitochondria. Binds to IGFBP3 and specifically blocks IGFBP3-induced cell death Induces chemotaxis of mononuclear phagocytes via FPR2. Reduces the aggregation and fibrillary formation by suppressing the effect of APP on mononuclear phagocytes and acts by competitively inhibiting the access of FPRL1 to APP.<ref>PMID:11371646</ref> <ref>PMID:14561895</ref> <ref>PMID:11717357</ref> <ref>PMID:12732850</ref> <ref>PMID:15153530</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 17:		Line 19:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Benaki, D.]]	+	[[Category: Benaki, D]]
-	[[Category: Evangelou, A.]]	+	[[Category: Evangelou, A]]
-	[[Category: Livaniou, E.]]	+	[[Category: Livaniou, E]]
-	[[Category: Mikros, E.]]	+	[[Category: Mikros, E]]
-	[[Category: Pelecanou, M.]]	+	[[Category: Pelecanou, M]]
-	[[Category: Vlassi, M.]]	+	[[Category: Vlassi, M]]
-	[[Category: Zikos, C.]]	+	[[Category: Zikos, C]]
	[[Category: Alzheimer's disease]]		[[Category: Alzheimer's disease]]
	[[Category: Humanin]]		[[Category: Humanin]]

OCA at 08:28, 8 October 2014

2014-10-08T08:28:34Z

←Older revision		Revision as of 08:28, 8 October 2014
Line 1:		Line 1:
-	[[~~Image~~:1y32.~~png\|left\|200px~~]]	+	==NMR structure of humanin in 30% TFE solution==
		+	<StructureSection load='1y32' size='340' side='right' caption='[[1y32]], [[NMR_Ensembles_of_Models \| 14 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1y32]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y32 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Y32 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=1y32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y32 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1y32 RCSB], [http://www.ebi.ac.uk/pdbsum/1y32 PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Humanin is a newly identified 24-residue peptide that suppresses neuronal cell death caused by a wide spectrum of familial Alzheimer's disease genes and the beta-amyloid peptide. In this study, NMR and circular dichroism studies of synthetic humanin in aqueous and 30% 2,2,2-trifluoroethanol (TFE) solutions are reported. In aqueous solution, humanin exists predominantly in an unstructured conformation in equilibrium with turn-like structures involving residues Gly5 to Leu10 and Glu15 to Leu18, providing indication of nascent helix. In the less polar environment of 30% TFE, humanin readily adopts helical structure with long-range order spanning residues Gly5 to Leu18. Comparative 3D modeling studies and topology predictions are in qualitative agreement with the experimental findings in both environments. Our studies reveal a flexible peptide in aqueous environment, which is free to interact with possible receptors that mediate its action, but may also acquire a helical conformation necessary for specific interactions and/or passage through membranes.

-	~~{{STRUCTURE_1y32\| PDB=1y32 \| SCENE= }}~~	+	Solution structure of humanin, a peptide against Alzheimer's disease-related neurotoxicity.,Benaki D, Zikos C, Evangelou A, Livaniou E, Vlassi M, Mikros E, Pelecanou M Biochem Biophys Res Commun. 2005 Apr 1;329(1):152-60. PMID:15721287<ref>PMID:15721287</ref>

-	~~===NMR structure~~ of ~~humanin in 30% TFE solution===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_15721287}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1y32]] is a 1 chain structure~~. ~~Full experimental information is available from [http://oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=1Y32 OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:015721287<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Benaki, D.]]		[[Category: Benaki, D.]]
	[[Category: Evangelou, A.]]		[[Category: Evangelou, A.]]

OCA: Protected "1y32" [edit=sysop:move=sysop]

2013-01-05T13:00:17Z

Protected "1y32" [edit=sysop:move=sysop]

←Older revision

Revision as of 13:00, 5 January 2013

OCA at 13:00, 5 January 2013

2013-01-05T13:00:15Z

←Older revision		Revision as of 13:00, 5 January 2013
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-	{{Seed}}
	[[Image:1y32.png\|left\|200px]]		[[Image:1y32.png\|left\|200px]]

-	<!--
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	{{STRUCTURE_1y32\| PDB=1y32 \| SCENE= }}		{{STRUCTURE_1y32\| PDB=1y32 \| SCENE= }}

	===NMR structure of humanin in 30% TFE solution===		===NMR structure of humanin in 30% TFE solution===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_15721287}}, adds the Publication Abstract to the page
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	{{ABSTRACT_PUBMED_15721287}}		{{ABSTRACT_PUBMED_15721287}}

	==About this Structure==		==About this Structure==
-	~~1Y32 is a~~ [[~~Single protein~~]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y32 OCA].	+	[[1y32]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y32 OCA].

	==Reference==		==Reference==
-	Solution structure of humanin, a peptide against Alzheimer's disease-related neurotoxicity., Benaki D, Zikos C, Evangelou A, Livaniou E, Vlassi M, Mikros E, Pelecanou M, Biochem Biophys Res Commun. 2005 Apr 1;329(1):152-60. PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/15721287 15721287]~~	+	<ref group="xtra">PMID:015721287</ref><references group="xtra"/>
-	~~[[Category: Single protein]]~~	+
	[[Category: Benaki, D.]]		[[Category: Benaki, D.]]
	[[Category: Evangelou, A.]]		[[Category: Evangelou, A.]]
Line 36:		Line 23:
	[[Category: Neuroprotection]]		[[Category: Neuroprotection]]
	[[Category: Nmr solution structure]]		[[Category: Nmr solution structure]]
-		+	[[Category: Unknown function]]
-	~~''Page seeded by~~ [~~http~~:~~//oca.weizmann.ac.il/oca OCA~~ ] ~~on Mon Jul 28 06:42:04 2008''~~	+

OCA at 03:42, 28 July 2008

2008-07-28T03:42:07Z

←Older revision		Revision as of 03:42, 28 July 2008
Line 1:		Line 1:
-	[[Image:1y32.~~gif~~\|left\|200px]]	+	{{Seed}}
		+	[[Image:1y32.png\|left\|200px]]

	<!--		<!--
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	{{STRUCTURE_1y32\| PDB=1y32 \| SCENE= }}		{{STRUCTURE_1y32\| PDB=1y32 \| SCENE= }}

-	~~'''~~NMR structure of humanin in 30% TFE solution~~'''~~	+	===NMR structure of humanin in 30% TFE solution===


-	~~==Overview==~~	+	<!--
-	~~Humanin is a newly identified 24~~-~~residue peptide that suppresses neuronal cell death caused by a wide spectrum of familial Alzheimer's disease genes and the beta~~-~~amyloid peptide. In~~ this ~~study~~, ~~NMR and circular dichroism studies of synthetic humanin in aqueous and 30% 2~~,2,2-trifluoroethanol (TFE) solutions are reported. In aqueous solution, humanin exists predominantly in an unstructured conformation in equilibrium with turn-like structures involving residues Gly5 to Leu10 and Glu15 to Leu18, providing indication of nascent helix. In the ~~less polar environment of 30% TFE, humanin readily adopts helical structure with long-range order spanning residues Gly5~~ to ~~Leu18. Comparative 3D modeling studies and topology predictions are in qualitative agreement with~~ the ~~experimental findings in both environments~~. ~~Our studies reveal a flexible peptide in aqueous environment~~, ~~which~~ is ~~free to interact with possible receptors that mediate its action, but may also acquire a helical conformation necessary for specific interactions and/or passage through membranes~~.	+	The line below this paragraph, {{ABSTRACT_PUBMED_15721287}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 15721287 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_15721287}}

	==About this Structure==		==About this Structure==
-	1Y32 is a [[Single protein]] structure. Full ~~crystallographic~~ information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y32 OCA].	+	1Y32 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y32 OCA].

	==Reference==		==Reference==
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	[[Category: Neuroprotection]]		[[Category: Neuroprotection]]
	[[Category: Nmr solution structure]]		[[Category: Nmr solution structure]]
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 15~~:49:33 2008''	+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:42:04 2008''