1g26 - Revision history

OCA at 07:11, 9 August 2023

OCA — Wed, 09 Aug 2023 07:11:21 GMT

←Older revision		Revision as of 07:11, 9 August 2023
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	==THE SOLUTION STRUCTURE OF A WELL-FOLDED PEPTIDE BASED ON THE 31-RESIDUE AMINO-TERMINAL SUBDOMAIN OF HUMAN GRANULIN A==		==THE SOLUTION STRUCTURE OF A WELL-FOLDED PEPTIDE BASED ON THE 31-RESIDUE AMINO-TERMINAL SUBDOMAIN OF HUMAN GRANULIN A==
-	<StructureSection load='1g26' size='340' side='right'caption='[[1g26~~]], [[NMR_Ensembles_of_Models \| 10 NMR models~~]]' scene=''>	+	<StructureSection load='1g26' size='340' side='right'caption='[[1g26]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1g26]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G26 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G26 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1g26]] 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=1G26 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G26 FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style~~=~~'overflow: auto; max-height: 3em;'>[[1qgm\|1qgm]], [[1fwo\|1fwo]]</div~~></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=1g26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g26 OCA], [https://pdbe.org/1g26 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g26 RCSB], [https://www.ebi.ac.uk/pdbsum/1g26 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g26 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=1g26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g26 OCA], [https://pdbe.org/1g26 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g26 RCSB], [https://www.ebi.ac.uk/pdbsum/1g26 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g26 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/GRN_HUMAN GRN_HUMAN]] Defects in GRN are the cause of ubiquitin-positive frontotemporal dementia (UP-FTD) [MIM:[https://omim.org/entry/607485 607485]]; also known as tau-negative frontotemporal dementia linked to chromosome 17. Frontotemporal dementia (FTD) is the second most common cause of dementia in people under the age of 65 years. It is an autosomal dominant neurodegenerative disease.<ref>PMID:16862116</ref> <ref>PMID:16983685</ref> <ref>PMID:18183624</ref> Defects in GRN are the cause of neuronal ceroid lipofuscinosis type 11 (CLN11) [MIM:[https://omim.org/entry/614706 614706]]. A form of neuronal ceroid lipofuscinosis characterized by rapidly progressive visual loss due to retinal dystrophy, seizures, cerebellar ataxia, and cerebellar atrophy. Cognitive decline may also occur. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material.<ref>PMID:22608501</ref>	+	[https://www.uniprot.org/uniprot/GRN_HUMAN GRN_HUMAN] Defects in GRN are the cause of ubiquitin-positive frontotemporal dementia (UP-FTD) [MIM:[https://omim.org/entry/607485 607485]; also known as tau-negative frontotemporal dementia linked to chromosome 17. Frontotemporal dementia (FTD) is the second most common cause of dementia in people under the age of 65 years. It is an autosomal dominant neurodegenerative disease.<ref>PMID:16862116</ref> <ref>PMID:16983685</ref> <ref>PMID:18183624</ref> Defects in GRN are the cause of neuronal ceroid lipofuscinosis type 11 (CLN11) [MIM:[https://omim.org/entry/614706 614706]. A form of neuronal ceroid lipofuscinosis characterized by rapidly progressive visual loss due to retinal dystrophy, seizures, cerebellar ataxia, and cerebellar atrophy. Cognitive decline may also occur. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material.<ref>PMID:22608501</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/GRN_HUMAN GRN_HUMAN]] Granulins have possible cytokine-like activity. They may play a role in inflammation, wound repair, and tissue remodeling. Granulin-4 promotes proliferation of the epithelial cell line A431 in culture while granulin-3 acts as an antagonist to granulin-4, inhibiting the growth.	+	[https://www.uniprot.org/uniprot/GRN_HUMAN GRN_HUMAN] Granulins have possible cytokine-like activity. They may play a role in inflammation, wound repair, and tissue remodeling. Granulin-4 promotes proliferation of the epithelial cell line A431 in culture while granulin-3 acts as an antagonist to granulin-4, inhibiting the growth.
	<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: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Ng, A]]	+	[[Category: Ng A]]
-	[[Category: Ni, F]]	+	[[Category: Ni F]]
-	[[Category: Tolkatchev, D]]	+	[[Category: Tolkatchev D]]
-	[[Category: Vranken, W]]	+	[[Category: Vranken W]]
-	~~[[Category: Beta-hairpin stack]]~~	+
-	~~[[Category: Cytokine]]~~	+
-	~~[[Category: Granulin/epithelin protein repeat~~]]	+

OCA at 07:10, 24 March 2021

OCA — Wed, 24 Mar 2021 07:10:52 GMT

←Older revision		Revision as of 07:10, 24 March 2021
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	<StructureSection load='1g26' size='340' side='right'caption='[[1g26]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>		<StructureSection load='1g26' size='340' side='right'caption='[[1g26]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1g26]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G26 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1G26 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1g26]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G26 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G26 FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qgm\|1qgm]], [[1fwo\|1fwo]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1qgm\|1qgm]], [[1fwo\|1fwo]]</div></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=1g26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g26 OCA], [~~http~~://pdbe.org/1g26 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1g26 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1g26 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1g26 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=1g26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g26 OCA], [https://pdbe.org/1g26 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g26 RCSB], [https://www.ebi.ac.uk/pdbsum/1g26 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g26 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/GRN_HUMAN GRN_HUMAN]] Defects in GRN are the cause of ubiquitin-positive frontotemporal dementia (UP-FTD) [MIM:[~~http~~://omim.org/entry/607485 607485]]; also known as tau-negative frontotemporal dementia linked to chromosome 17. Frontotemporal dementia (FTD) is the second most common cause of dementia in people under the age of 65 years. It is an autosomal dominant neurodegenerative disease.<ref>PMID:16862116</ref> <ref>PMID:16983685</ref> <ref>PMID:18183624</ref> Defects in GRN are the cause of neuronal ceroid lipofuscinosis type 11 (CLN11) [MIM:[~~http~~://omim.org/entry/614706 614706]]. A form of neuronal ceroid lipofuscinosis characterized by rapidly progressive visual loss due to retinal dystrophy, seizures, cerebellar ataxia, and cerebellar atrophy. Cognitive decline may also occur. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material.<ref>PMID:22608501</ref>	+	[[https://www.uniprot.org/uniprot/GRN_HUMAN GRN_HUMAN]] Defects in GRN are the cause of ubiquitin-positive frontotemporal dementia (UP-FTD) [MIM:[https://omim.org/entry/607485 607485]]; also known as tau-negative frontotemporal dementia linked to chromosome 17. Frontotemporal dementia (FTD) is the second most common cause of dementia in people under the age of 65 years. It is an autosomal dominant neurodegenerative disease.<ref>PMID:16862116</ref> <ref>PMID:16983685</ref> <ref>PMID:18183624</ref> Defects in GRN are the cause of neuronal ceroid lipofuscinosis type 11 (CLN11) [MIM:[https://omim.org/entry/614706 614706]]. A form of neuronal ceroid lipofuscinosis characterized by rapidly progressive visual loss due to retinal dystrophy, seizures, cerebellar ataxia, and cerebellar atrophy. Cognitive decline may also occur. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material.<ref>PMID:22608501</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/GRN_HUMAN GRN_HUMAN]] Granulins have possible cytokine-like activity. They may play a role in inflammation, wound repair, and tissue remodeling. Granulin-4 promotes proliferation of the epithelial cell line A431 in culture while granulin-3 acts as an antagonist to granulin-4, inhibiting the growth.	+	[[https://www.uniprot.org/uniprot/GRN_HUMAN GRN_HUMAN]] Granulins have possible cytokine-like activity. They may play a role in inflammation, wound repair, and tissue remodeling. Granulin-4 promotes proliferation of the epithelial cell line A431 in culture while granulin-3 acts as an antagonist to granulin-4, inhibiting the growth.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 06:54, 19 June 2019

OCA — Wed, 19 Jun 2019 06:54:15 GMT

←Older revision		Revision as of 06:54, 19 June 2019
Line 1:		Line 1:

	==THE SOLUTION STRUCTURE OF A WELL-FOLDED PEPTIDE BASED ON THE 31-RESIDUE AMINO-TERMINAL SUBDOMAIN OF HUMAN GRANULIN A==		==THE SOLUTION STRUCTURE OF A WELL-FOLDED PEPTIDE BASED ON THE 31-RESIDUE AMINO-TERMINAL SUBDOMAIN OF HUMAN GRANULIN A==
-	<StructureSection load='1g26' size='340' side='right' caption='[[1g26]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>	+	<StructureSection load='1g26' size='340' side='right'caption='[[1g26]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1g26]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G26 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G26 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1g26]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G26 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G26 FirstGlance]. <br>
Line 24:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Ng, A]]		[[Category: Ng, A]]
	[[Category: Ni, F]]		[[Category: Ni, F]]

OCA at 10:47, 13 September 2017

OCA — Wed, 13 Sep 2017 10:47:40 GMT

←Older revision		Revision as of 10:47, 13 September 2017
Line 1:		Line 1:
		+
	==THE SOLUTION STRUCTURE OF A WELL-FOLDED PEPTIDE BASED ON THE 31-RESIDUE AMINO-TERMINAL SUBDOMAIN OF HUMAN GRANULIN A==		==THE SOLUTION STRUCTURE OF A WELL-FOLDED PEPTIDE BASED ON THE 31-RESIDUE AMINO-TERMINAL SUBDOMAIN OF HUMAN GRANULIN A==
	<StructureSection load='1g26' size='340' side='right' caption='[[1g26]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>		<StructureSection load='1g26' size='340' side='right' caption='[[1g26]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[1g26]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G26 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G26 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1g26]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G26 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G26 FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qgm\|1qgm]], [[1fwo\|1fwo]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qgm\|1qgm]], [[1fwo\|1fwo]]</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=1g26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g26 OCA], [http://pdbe.org/1g26 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g26 RCSB], [http://www.ebi.ac.uk/pdbsum/1g26 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=1g26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g26 OCA], [http://pdbe.org/1g26 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g26 RCSB], [http://www.ebi.ac.uk/pdbsum/1g26 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1g26 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==

OCA at 08:17, 11 September 2015

OCA — Fri, 11 Sep 2015 08:17:29 GMT

←Older revision		Revision as of 08:17, 11 September 2015
Line 4:		Line 4:
	<table><tr><td colspan='2'>[[1g26]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G26 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G26 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1g26]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G26 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G26 FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qgm\|1qgm]], [[1fwo\|1fwo]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qgm\|1qgm]], [[1fwo\|1fwo]]</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=1g26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g26 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1g26 RCSB], [http://www.ebi.ac.uk/pdbsum/1g26 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=1g26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g26 OCA], [http://pdbe.org/1g26 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g26 RCSB], [http://www.ebi.ac.uk/pdbsum/1g26 PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 18:		Line 18:
	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 1g26" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:39, 18 December 2014

OCA — Thu, 18 Dec 2014 11:39:58 GMT

←Older revision		Revision as of 11:39, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1g26\| PDB=1g26 \| SCENE= }}~~	+	==THE SOLUTION STRUCTURE OF A WELL-FOLDED PEPTIDE BASED ON THE 31-RESIDUE AMINO-TERMINAL SUBDOMAIN OF HUMAN GRANULIN A==
-	===THE SOLUTION STRUCTURE OF A WELL-FOLDED PEPTIDE BASED ON THE 31-RESIDUE AMINO-TERMINAL SUBDOMAIN OF HUMAN GRANULIN A===	+	<StructureSection load='1g26' size='340' side='right' caption='[[1g26]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
-	~~{{ABSTRACT_PUBMED_10715107}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[1g26]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G26 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G26 FirstGlance]. <br>
-	==Disease==	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qgm\|1qgm]], [[1fwo\|1fwo]]</td></tr>
-	[[http://www.uniprot.org/uniprot/GRN_HUMAN GRN_HUMAN]] Defects in GRN are the cause of ubiquitin-positive frontotemporal dementia (UP-FTD) [MIM:[http://omim.org/entry/607485 607485]]; also known as tau-negative frontotemporal dementia linked to chromosome 17. Frontotemporal dementia (FTD) is the second most common cause of dementia in people under the age of 65 years. It is an autosomal dominant neurodegenerative disease.<ref>PMID:16862116</ref><ref>PMID:16983685</ref><ref>PMID:18183624</ref> Defects in GRN are the cause of neuronal ceroid lipofuscinosis type 11 (CLN11) [MIM:[http://omim.org/entry/614706 614706]]. A form of neuronal ceroid lipofuscinosis characterized by rapidly progressive visual loss due to retinal dystrophy, seizures, cerebellar ataxia, and cerebellar atrophy. Cognitive decline may also occur. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material.<ref>PMID:22608501</ref>	+	<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=1g26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g26 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1g26 RCSB], [http://www.ebi.ac.uk/pdbsum/1g26 PDBsum]</span></td></tr>
-		+	</table>
-	==Function==	+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/GRN_HUMAN GRN_HUMAN]] Defects in GRN are the cause of ubiquitin-positive frontotemporal dementia (UP-FTD) [MIM:[http://omim.org/entry/607485 607485]]; also known as tau-negative frontotemporal dementia linked to chromosome 17. Frontotemporal dementia (FTD) is the second most common cause of dementia in people under the age of 65 years. It is an autosomal dominant neurodegenerative disease.<ref>PMID:16862116</ref> <ref>PMID:16983685</ref> <ref>PMID:18183624</ref> Defects in GRN are the cause of neuronal ceroid lipofuscinosis type 11 (CLN11) [MIM:[http://omim.org/entry/614706 614706]]. A form of neuronal ceroid lipofuscinosis characterized by rapidly progressive visual loss due to retinal dystrophy, seizures, cerebellar ataxia, and cerebellar atrophy. Cognitive decline may also occur. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material.<ref>PMID:22608501</ref>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/GRN_HUMAN GRN_HUMAN]] Granulins have possible cytokine-like activity. They may play a role in inflammation, wound repair, and tissue remodeling. Granulin-4 promotes proliferation of the epithelial cell line A431 in culture while granulin-3 acts as an antagonist to granulin-4, inhibiting the growth.		[[http://www.uniprot.org/uniprot/GRN_HUMAN GRN_HUMAN]] Granulins have possible cytokine-like activity. They may play a role in inflammation, wound repair, and tissue remodeling. Granulin-4 promotes proliferation of the epithelial cell line A431 in culture while granulin-3 acts as an antagonist to granulin-4, inhibiting the growth.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Four amino acid substitutions were introduced into a peptide corresponding to the amino-terminal subdomain (30-31 residues) of human granulin A (HGA) in order to assess the contributions of a hydrophobic framework and other interactions to structure stabilization of the stack of two beta-hairpins. The resulting hybrid peptide, HGA 1-31 (D1V, K3H, S9I, Q20P) with four free cysteines, spontaneously formed a uniquely disulfide-bonded isomer with an expected [1-3, 2-4] disulfide pairing pattern. This peptide was characterized in detail by use of NMR and shown to assume a highly stable structure in solution, in contrast to the amino-terminal 1-30 fragment of human granulin A. The prototype peptide, or HGA 1-30 (C17S, C27S), had lower resistance to chemical reduction and proteolysis, broad NH and H(alpha) proton resonances, lower proton resonance dispersion, and no slowly exchanging amide protons. Two other peptides, HGA 1-30 (C17S, Q20P, C27S) and HGA 1-31 (D1V, K3H, S9I, C17S, C27S), with either Pro20 stabilizing a potential reverse turn or with a hydrophobic cluster consisting of Val1, His3, and Ile9, had sharper and slightly better dispersed NH and H(alpha) proton resonances, but still no slowly exchanging amide protons. The solution structure of HGA 1-31 (D1V, K3H, S9I, Q20P) indicates that it adopts a well-folded conformation of a stack of two beta-hairpins, as found for the amino-terminal subdomain of the prototypic carp granulin-1 with representative beta-hairpin stacks. These results highlight the importance of both hydrophobic and turn-stabilizing interactions for the structural integrity of the hairpin stack scaffold. The conformational stability appears to be maintained by a combination of the well-formed second beta-hairpin and two hydrophobic clusters, one located at the interface between the two beta-hairpins and the other on "top" of the first beta-hairpin. The implications of these findings for the design of conformationally stable hairpin stacks are discussed.

-	~~==About this Structure==~~	+	Design and solution structure of a well-folded stack of two beta-hairpins based on the amino-terminal fragment of human granulin A.,Tolkatchev D, Ng A, Vranken W, Ni F Biochemistry. 2000 Mar 21;39(11):2878-86. PMID:10715107<ref>PMID:10715107</ref>
-	~~[[1g26]] is a 1 chain~~ structure. ~~Full experimental information is available from [http://oca~~.~~weizmann.ac.il/oca~~-~~bin/ocashort?id=1G26 OCA]~~.	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:010715107</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
-	[[Category: Ng, A.]]	+	== References ==
-	[[Category: Ni, F.]]	+	<references/>
-	[[Category: Tolkatchev, D.]]	+	__TOC__
-	[[Category: Vranken, W.]]	+	</StructureSection>
		+	[[Category: Ng, A]]
		+	[[Category: Ni, F]]
		+	[[Category: Tolkatchev, D]]
		+	[[Category: Vranken, W]]
	[[Category: Beta-hairpin stack]]		[[Category: Beta-hairpin stack]]
	[[Category: Cytokine]]		[[Category: Cytokine]]
	[[Category: Granulin/epithelin protein repeat]]		[[Category: Granulin/epithelin protein repeat]]

OCA at 04:21, 25 March 2013

OCA — Mon, 25 Mar 2013 04:21:56 GMT

←Older revision		Revision as of 04:21, 25 March 2013
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-	[[Image:1g26.png\|left\|200px]]
-
	{{STRUCTURE_1g26\| PDB=1g26 \| SCENE= }}		{{STRUCTURE_1g26\| PDB=1g26 \| SCENE= }}
-
	===THE SOLUTION STRUCTURE OF A WELL-FOLDED PEPTIDE BASED ON THE 31-RESIDUE AMINO-TERMINAL SUBDOMAIN OF HUMAN GRANULIN A===		===THE SOLUTION STRUCTURE OF A WELL-FOLDED PEPTIDE BASED ON THE 31-RESIDUE AMINO-TERMINAL SUBDOMAIN OF HUMAN GRANULIN A===
		+	{{ABSTRACT_PUBMED_10715107}}

-	~~{{ABSTRACT_PUBMED_10715107}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/GRN_HUMAN GRN_HUMAN]] Defects in GRN are the cause of ubiquitin-positive frontotemporal dementia (UP-FTD) [MIM:[http://omim.org/entry/607485 607485]]; also known as tau-negative frontotemporal dementia linked to chromosome 17. Frontotemporal dementia (FTD) is the second most common cause of dementia in people under the age of 65 years. It is an autosomal dominant neurodegenerative disease.<ref>PMID:16862116</ref><ref>PMID:16983685</ref><ref>PMID:18183624</ref> Defects in GRN are the cause of neuronal ceroid lipofuscinosis type 11 (CLN11) [MIM:[http://omim.org/entry/614706 614706]]. A form of neuronal ceroid lipofuscinosis characterized by rapidly progressive visual loss due to retinal dystrophy, seizures, cerebellar ataxia, and cerebellar atrophy. Cognitive decline may also occur. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material.<ref>PMID:22608501</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/GRN_HUMAN GRN_HUMAN]] Granulins have possible cytokine-like activity. They may play a role in inflammation, wound repair, and tissue remodeling. Granulin-4 promotes proliferation of the epithelial cell line A431 in culture while granulin-3 acts as an antagonist to granulin-4, inhibiting the growth.

	==About this Structure==		==About this Structure==
Line 11:		Line 13:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:010715107</ref><references group="xtra"/>	+	<ref group="xtra">PMID:010715107</ref><references group="xtra"/><references/>
	[[Category: Ng, A.]]		[[Category: Ng, A.]]
	[[Category: Ni, F.]]		[[Category: Ni, F.]]

OCA: Protected "1g26" [edit=sysop:move=sysop]

OCA — Tue, 14 Aug 2012 17:31:47 GMT

Protected "1g26" [edit=sysop:move=sysop]

←Older revision

Revision as of 17:31, 14 August 2012

OCA at 17:31, 14 August 2012

OCA — Tue, 14 Aug 2012 17:31:45 GMT

←Older revision		Revision as of 17:31, 14 August 2012
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-	{{Seed}}
	[[Image:1g26.png\|left\|200px]]		[[Image:1g26.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1g26", 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.
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	{{STRUCTURE_1g26\| PDB=1g26 \| SCENE= }}		{{STRUCTURE_1g26\| PDB=1g26 \| SCENE= }}

	===THE SOLUTION STRUCTURE OF A WELL-FOLDED PEPTIDE BASED ON THE 31-RESIDUE AMINO-TERMINAL SUBDOMAIN OF HUMAN GRANULIN A===		===THE SOLUTION STRUCTURE OF A WELL-FOLDED PEPTIDE BASED ON THE 31-RESIDUE AMINO-TERMINAL SUBDOMAIN OF HUMAN GRANULIN A===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_10715107}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 10715107 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_10715107}}		{{ABSTRACT_PUBMED_10715107}}

	==About this Structure==		==About this Structure==
-	~~1G26 is a~~ [[~~Single protein~~]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G26 OCA].	+	[[1g26]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G26 OCA].

	==Reference==		==Reference==
-	Design and solution structure of a well-folded stack of two beta-hairpins based on the amino-terminal fragment of human granulin A., Tolkatchev D, Ng A, Vranken W, Ni F, Biochemistry. 2000 Mar 21;39(11):2878-86. PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/10715107 10715107]~~	+	<ref group="xtra">PMID:010715107</ref><references group="xtra"/>
-	~~[[Category: Single protein]]~~	+
	[[Category: Ng, A.]]		[[Category: Ng, A.]]
	[[Category: Ni, F.]]		[[Category: Ni, F.]]
Line 30:		Line 17:
	[[Category: Vranken, W.]]		[[Category: Vranken, W.]]
	[[Category: Beta-hairpin stack]]		[[Category: Beta-hairpin stack]]
		+	[[Category: Cytokine]]
	[[Category: Granulin/epithelin protein repeat]]		[[Category: Granulin/epithelin protein repeat]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:17:50 2008''

OCA at 01:17, 1 July 2008

OCA — Tue, 01 Jul 2008 01:17:52 GMT

←Older revision		Revision as of 01:17, 1 July 2008
Line 1:		Line 1:
-	[[Image:1g26.~~gif~~\|left\|200px]]	+	{{Seed}}
		+	[[Image:1g26.png\|left\|200px]]

	<!--		<!--
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	{{STRUCTURE_1g26\| PDB=1g26 \| SCENE= }}		{{STRUCTURE_1g26\| PDB=1g26 \| SCENE= }}

-	~~'''~~THE SOLUTION STRUCTURE OF A WELL-FOLDED PEPTIDE BASED ON THE 31-RESIDUE AMINO-TERMINAL SUBDOMAIN OF HUMAN GRANULIN A~~'''~~	+	===THE SOLUTION STRUCTURE OF A WELL-FOLDED PEPTIDE BASED ON THE 31-RESIDUE AMINO-TERMINAL SUBDOMAIN OF HUMAN GRANULIN A===


-	~~==Overview==~~	+	<!--
-	~~Four amino acid substitutions were introduced into a peptide corresponding to the amino~~-~~terminal subdomain (30~~-~~31 residues) of human granulin A (HGA) in order to assess the contributions of a hydrophobic framework and other interactions to structure stabilization of the stack of two beta-hairpins.~~ The ~~resulting hybrid peptide~~, ~~HGA 1-31 (D1V~~, K3H, S9I, Q20P) with four free cysteines, spontaneously formed a uniquely disulfide-bonded isomer with an expected [1-3, 2-4] disulfide pairing pattern. This peptide was characterized in detail by use of NMR and shown to assume a highly stable structure in solution, in contrast to the ~~amino-terminal 1-30 fragment of human granulin A. The prototype peptide, or HGA 1-30~~ (~~C17S, C27S), had lower resistance to chemical reduction and proteolysis, broad NH and H(alpha) proton resonances, lower proton resonance dispersion, and no slowly exchanging amide protons~~. Two other peptides, HGA 1-30 (C17S, Q20P, C27S) and HGA 1-31 (D1V, K3H, S9I, C17S, C27S), with either Pro20 stabilizing a potential reverse turn or with a hydrophobic cluster consisting of Val1, His3, and Ile9, had sharper and slightly better dispersed NH and H(alpha) proton resonances, but still no slowly exchanging amide protons. ~~The solution structure of HGA 1-31 (D1V, K3H, S9I, Q20P~~) ~~indicates that it adopts a well-folded conformation of a stack of two beta-hairpins~~, ~~as found for~~ the ~~amino-terminal subdomain of the prototypic carp granulin-1 with representative beta-hairpin stacks~~. ~~These results highlight the importance of both hydrophobic and turn~~-~~stabilizing interactions for the structural integrity of the hairpin stack scaffold. The conformational stability appears to be maintained by a combination of the well~~-formed second beta-hairpin and two hydrophobic clusters, one located at the interface between the two beta-hairpins and the other on "top" of the first beta-hairpin. The implications of these findings for the design of conformationally stable hairpin stacks are discussed.	+	The line below this paragraph, {{ABSTRACT_PUBMED_10715107}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 10715107 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_10715107}}

	==About this Structure==		==About this Structure==
-	1G26 is a [[Single protein]] structure. Full ~~crystallographic~~ information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G26 OCA].	+	1G26 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G26 OCA].

	==Reference==		==Reference==
Line 27:		Line 31:
	[[Category: Beta-hairpin stack]]		[[Category: Beta-hairpin stack]]
	[[Category: Granulin/epithelin protein repeat]]		[[Category: Granulin/epithelin protein repeat]]
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 17~~:02:34 2008''	+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:17:50 2008''