3edy - Revision history

OCA at 11:47, 16 February 2022

OCA — Wed, 16 Feb 2022 11:47:27 GMT

←Older revision		Revision as of 11:47, 16 February 2022
Line 1:		Line 1:

	==Crystal Structure of the Precursor Form of Human Tripeptidyl-Peptidase 1==		==Crystal Structure of the Precursor Form of Human Tripeptidyl-Peptidase 1==
-	<StructureSection load='3edy' size='340' side='right' caption='[[3edy]], [[Resolution\|resolution]] 1.85Å' scene=''>	+	<StructureSection load='3edy' size='340' side='right'caption='[[3edy]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3edy]] 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=3EDY OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3EDY FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3edy]] 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=3EDY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EDY FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TPP1, CLN2 ([~~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">TPP1, CLN2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Tripeptidyl-peptidase_I Tripeptidyl-peptidase I], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.9 3.4.14.9] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Tripeptidyl-peptidase_I Tripeptidyl-peptidase I], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.9 3.4.14.9] </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=3edy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3edy OCA], [~~http~~://pdbe.org/3edy PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3edy RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3edy PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3edy 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=3edy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3edy OCA], [https://pdbe.org/3edy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3edy RCSB], [https://www.ebi.ac.uk/pdbsum/3edy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3edy ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/TPP1_HUMAN TPP1_HUMAN]] Defects in TPP1 are the cause of neuronal ceroid lipofuscinosis type 2 (CLN2) [MIM:[~~http~~://omim.org/entry/204500 204500]]. A form of neuronal ceroid lipofuscinosis. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy. The lipopigment pattern seen most often in CLN2 consists of curvilinear profiles.<ref>PMID:9295267</ref> <ref>PMID:10330339</ref> <ref>PMID:10665500</ref> <ref>PMID:11339651</ref> <ref>PMID:11241479</ref> <ref>PMID:11589012</ref> <ref>PMID:12376936</ref> <ref>PMID:12414822</ref> <ref>PMID:12698559</ref> <ref>PMID:14736728</ref> <ref>PMID:19201763</ref> <ref>PMID:20340139</ref> <ref>PMID:21990111</ref>	+	[[https://www.uniprot.org/uniprot/TPP1_HUMAN TPP1_HUMAN]] Defects in TPP1 are the cause of neuronal ceroid lipofuscinosis type 2 (CLN2) [MIM:[https://omim.org/entry/204500 204500]]. A form of neuronal ceroid lipofuscinosis. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy. The lipopigment pattern seen most often in CLN2 consists of curvilinear profiles.<ref>PMID:9295267</ref> <ref>PMID:10330339</ref> <ref>PMID:10665500</ref> <ref>PMID:11339651</ref> <ref>PMID:11241479</ref> <ref>PMID:11589012</ref> <ref>PMID:12376936</ref> <ref>PMID:12414822</ref> <ref>PMID:12698559</ref> <ref>PMID:14736728</ref> <ref>PMID:19201763</ref> <ref>PMID:20340139</ref> <ref>PMID:21990111</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/TPP1_HUMAN TPP1_HUMAN]] Lysosomal serine protease with tripeptidyl-peptidase I activity. May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. Requires substrates with an unsubstituted N-terminus (By similarity).	+	[[https://www.uniprot.org/uniprot/TPP1_HUMAN TPP1_HUMAN]] Lysosomal serine protease with tripeptidyl-peptidase I activity. May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. Requires substrates with an unsubstituted N-terminus (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ed/3edy_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ed/3edy_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 32:		Line 32:
	</div>		</div>
	<div class="pdbe-citations 3edy" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3edy" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Tripeptidyl peptidase\|Tripeptidyl peptidase]]
	== References ==		== References ==
	<references/>		<references/>
Line 37:		Line 40:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Tripeptidyl-peptidase I]]		[[Category: Tripeptidyl-peptidase I]]
	[[Category: Das, K]]		[[Category: Das, K]]

OCA at 09:08, 25 October 2017

OCA — Wed, 25 Oct 2017 09:08:56 GMT

←Older revision		Revision as of 09:08, 25 October 2017
Line 1:		Line 1:
		+
	==Crystal Structure of the Precursor Form of Human Tripeptidyl-Peptidase 1==		==Crystal Structure of the Precursor Form of Human Tripeptidyl-Peptidase 1==
	<StructureSection load='3edy' size='340' side='right' caption='[[3edy]], [[Resolution\|resolution]] 1.85Å' scene=''>		<StructureSection load='3edy' size='340' side='right' caption='[[3edy]], [[Resolution\|resolution]] 1.85Å' scene=''>
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	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TPP1, CLN2 ([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">TPP1, CLN2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tripeptidyl-peptidase_I Tripeptidyl-peptidase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.9 3.4.14.9] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tripeptidyl-peptidase_I Tripeptidyl-peptidase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.9 3.4.14.9] </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=3edy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3edy OCA], [http://pdbe.org/3edy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3edy RCSB], [http://www.ebi.ac.uk/pdbsum/3edy 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=3edy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3edy OCA], [http://pdbe.org/3edy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3edy RCSB], [http://www.ebi.ac.uk/pdbsum/3edy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3edy ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 31:		Line 32:
	</div>		</div>
	<div class="pdbe-citations 3edy" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3edy" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Aminopeptidase\|Aminopeptidase]]
-	*[[Tripeptidyl peptidase\|Tripeptidyl peptidase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 22:45, 8 February 2016

OCA — Mon, 08 Feb 2016 22:45:39 GMT

←Older revision		Revision as of 22:45, 8 February 2016
Line 2:		Line 2:
	<StructureSection load='3edy' size='340' side='right' caption='[[3edy]], [[Resolution\|resolution]] 1.85Å' scene=''>		<StructureSection load='3edy' size='340' side='right' caption='[[3edy]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3edy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EDY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EDY FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3edy]] 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=3EDY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EDY FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TPP1, CLN2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TPP1, CLN2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tripeptidyl-peptidase_I Tripeptidyl-peptidase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.9 3.4.14.9] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tripeptidyl-peptidase_I Tripeptidyl-peptidase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.9 3.4.14.9] </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=3edy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3edy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3edy RCSB], [http://www.ebi.ac.uk/pdbsum/3edy 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=3edy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3edy OCA], [http://pdbe.org/3edy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3edy RCSB], [http://www.ebi.ac.uk/pdbsum/3edy PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 20:		Line 20:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3edy ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 30:		Line 30:
	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 3edy" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 38:		Line 39:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Tripeptidyl-peptidase I]]		[[Category: Tripeptidyl-peptidase I]]
	[[Category: Das, K]]		[[Category: Das, K]]

OCA at 13:09, 18 December 2014

OCA — Thu, 18 Dec 2014 13:09:05 GMT

←Older revision		Revision as of 13:09, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3edy\| PDB=3edy \| SCENE= }}~~	+	==Crystal Structure of the Precursor Form of Human Tripeptidyl-Peptidase 1==
-	===Crystal Structure of the Precursor Form of Human Tripeptidyl-Peptidase 1===	+	<StructureSection load='3edy' size='340' side='right' caption='[[3edy]], [[Resolution\|resolution]] 1.85Å' scene=''>
-	~~{{ABSTRACT_PUBMED_19038967}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3edy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EDY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EDY FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TPP1, CLN2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tripeptidyl-peptidase_I Tripeptidyl-peptidase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.9 3.4.14.9] </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=3edy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3edy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3edy RCSB], [http://www.ebi.ac.uk/pdbsum/3edy PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/TPP1_HUMAN TPP1_HUMAN]] Defects in TPP1 are the cause of neuronal ceroid lipofuscinosis type 2 (CLN2) [MIM:[http://omim.org/entry/204500 204500]]. A form of neuronal ceroid lipofuscinosis. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy. The lipopigment pattern seen most often in CLN2 consists of curvilinear profiles.<ref>PMID:9295267</ref> <ref>PMID:10330339</ref> <ref>PMID:10665500</ref> <ref>PMID:11339651</ref> <ref>PMID:11241479</ref> <ref>PMID:11589012</ref> <ref>PMID:12376936</ref> <ref>PMID:12414822</ref> <ref>PMID:12698559</ref> <ref>PMID:14736728</ref> <ref>PMID:19201763</ref> <ref>PMID:20340139</ref> <ref>PMID:21990111</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/TPP1_HUMAN TPP1_HUMAN]] Lysosomal serine protease with tripeptidyl-peptidase I activity. May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. Requires substrates with an unsubstituted N-terminus (By similarity).
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ed/3edy_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Late infantile neuronal ceroid lipofuscinosis is a fatal childhood neurological disorder caused by a deficiency in the lysosomal protease tripeptidyl-peptidase 1 (TPP1). TPP1 represents the only known mammalian member of the S53 family of serine proteases, a group characterized by a subtilisin-like fold, a Ser-Glu-Asp catalytic triad, and an acidic pH optimum. TPP1 is synthesized as an inactive proenzyme (pro-TPP1) that is proteolytically processed into the active enzyme after exposure to low pH in vitro or targeting to the lysosome in vivo. In this study, we describe an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease. The crystal structure of deglycosylated pro-TPP1 was determined at 1.85 A resolution. A large 151-residue C-shaped prodomain makes extensive contacts as it wraps around the surface of the catalytic domain with the two domains connected by a 24-residue flexible linker that passes through the substrate-binding groove. The proenzyme structure reveals suboptimal catalytic triad geometry with its propiece linker partially blocking the substrate-binding site, which together serve to prevent premature activation of the protease. Finally, we have identified numerous processing intermediates and propose a structural model that explains the pathway for TPP1 activation in vitro. These data provide new insights into TPP1 function and represent a valuable resource for constructing improved TPP1 variants for treatment of late infantile neuronal ceroid lipofuscinosis.

-	~~==Disease==~~	+	Crystal Structure and Autoactivation Pathway of the Precursor Form of Human Tripeptidyl-peptidase 1, the Enzyme Deficient in Late Infantile Ceroid Lipofuscinosis.,Guhaniyogi J, Sohar I, Das K, Stock AM, Lobel P J Biol Chem. 2009 Feb 6;284(6):3985-97. Epub 2008 Nov 26. PMID:19038967<ref>PMID:19038967</ref>
-	~~[[http://www.uniprot.org/uniprot/TPP1_HUMAN TPP1_HUMAN]] Defects in TPP1 are~~ the ~~cause~~ of ~~neuronal ceroid lipofuscinosis type 2 (CLN2) [MIM:[http://omim~~.~~org/entry/204500 204500]]. A form of neuronal ceroid lipofuscinosis. Neuronal ceroid lipofuscinoses are progressive neurodegenerative~~, ~~lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material~~, ~~and clinically by seizures~~, ~~dementia~~, ~~visual loss~~, ~~and/or cerebral atrophy~~. ~~The lipopigment pattern seen most often in CLN2 consists of curvilinear profiles~~.~~<ref>~~PMID:9295267</ref><ref>PMID:10330339</ref><ref>PMID:10665500</ref><ref>PMID:11339651</ref><ref>PMID:11241479</ref><ref>PMID:11589012</ref><ref>PMID:12376936</ref><ref>PMID:12414822</ref><ref>PMID:12698559</ref><ref>PMID:14736728</ref><ref>PMID:19201763</ref><ref>PMID:20340139</ref><ref>PMID:~~21990111~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www.uniprot.org/uniprot/TPP1_HUMAN TPP1_HUMAN]] Lysosomal serine protease with tripeptidyl-peptidase I activity. May act as~~ a ~~non-specific lysosomal peptidase which generates tripeptides from~~ the ~~breakdown products produced by lysosomal proteinases~~. ~~Requires substrates with an unsubstituted N-terminus (By similarity)~~.	+	</div>
-		+
-	~~==About this Structure==~~	+
-	~~[[3edy]] is a 1 chain structure with sequence from [http:~~/~~/en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EDY OCA].~~	+

	==See Also==		==See Also==
		+	*[[Aminopeptidase\|Aminopeptidase]]
	*[[Tripeptidyl peptidase\|Tripeptidyl peptidase]]		*[[Tripeptidyl peptidase\|Tripeptidyl peptidase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:019038967</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Tripeptidyl-peptidase I]]		[[Category: Tripeptidyl-peptidase I]]
-	[[Category: Das, K.]]	+	[[Category: Das, K]]
-	[[Category: Guhaniyogi, J.]]	+	[[Category: Guhaniyogi, J]]
-	[[Category: Lobel, P.]]	+	[[Category: Lobel, P]]
-	[[Category: Sohar, I.]]	+	[[Category: Sohar, I]]
-	[[Category: Stock, A M.]]	+	[[Category: Stock, A M]]
	[[Category: Batten disease]]		[[Category: Batten disease]]
	[[Category: Catalytic triad]]		[[Category: Catalytic triad]]

OCA at 22:41, 24 March 2013

OCA — Sun, 24 Mar 2013 22:41:08 GMT

←Older revision		Revision as of 22:41, 24 March 2013
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-	[[Image:3edy.png\|left\|200px]]
-
	{{STRUCTURE_3edy\| PDB=3edy \| SCENE= }}		{{STRUCTURE_3edy\| PDB=3edy \| SCENE= }}
-
	===Crystal Structure of the Precursor Form of Human Tripeptidyl-Peptidase 1===		===Crystal Structure of the Precursor Form of Human Tripeptidyl-Peptidase 1===
		+	{{ABSTRACT_PUBMED_19038967}}

-	~~{{ABSTRACT_PUBMED_19038967}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/TPP1_HUMAN TPP1_HUMAN]] Defects in TPP1 are the cause of neuronal ceroid lipofuscinosis type 2 (CLN2) [MIM:[http://omim.org/entry/204500 204500]]. A form of neuronal ceroid lipofuscinosis. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy. The lipopigment pattern seen most often in CLN2 consists of curvilinear profiles.<ref>PMID:9295267</ref><ref>PMID:10330339</ref><ref>PMID:10665500</ref><ref>PMID:11339651</ref><ref>PMID:11241479</ref><ref>PMID:11589012</ref><ref>PMID:12376936</ref><ref>PMID:12414822</ref><ref>PMID:12698559</ref><ref>PMID:14736728</ref><ref>PMID:19201763</ref><ref>PMID:20340139</ref><ref>PMID:21990111</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/TPP1_HUMAN TPP1_HUMAN]] Lysosomal serine protease with tripeptidyl-peptidase I activity. May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. Requires substrates with an unsubstituted N-terminus (By similarity).

	==About this Structure==		==About this Structure==
Line 14:		Line 16:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:019038967</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019038967</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Tripeptidyl-peptidase I]]		[[Category: Tripeptidyl-peptidase I]]

OCA at 11:43, 20 October 2012

OCA — Sat, 20 Oct 2012 11:43:51 GMT

←Older revision		Revision as of 11:43, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3edy]] is a 1 chain structure ~~of [[Tripeptidyl peptidase]]~~ with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EDY OCA].	+	[[3edy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EDY OCA].

	==See Also==		==See Also==

OCA at 06:23, 26 July 2012

OCA — Thu, 26 Jul 2012 06:23:59 GMT

←Older revision		Revision as of 06:23, 26 July 2012
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	[[Image:3edy.png\|left\|200px]]		[[Image:3edy.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3edy", 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_3edy\| PDB=3edy \| SCENE= }}		{{STRUCTURE_3edy\| PDB=3edy \| SCENE= }}

	===Crystal Structure of the Precursor Form of Human Tripeptidyl-Peptidase 1===		===Crystal Structure of the Precursor Form of Human Tripeptidyl-Peptidase 1===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_19038967}}, adds the Publication Abstract to the page
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	{{ABSTRACT_PUBMED_19038967}}		{{ABSTRACT_PUBMED_19038967}}

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	==See Also==		==See Also==
-	*[[Tripeptidyl peptidase]]	+	*[[Tripeptidyl peptidase\|Tripeptidyl peptidase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~19038967~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019038967</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Tripeptidyl-peptidase I]]		[[Category: Tripeptidyl-peptidase I]]
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	[[Category: Sohar, I.]]		[[Category: Sohar, I.]]
	[[Category: Stock, A M.]]		[[Category: Stock, A M.]]
-	[[Category: Alternative splicing]]
	[[Category: Batten disease]]		[[Category: Batten disease]]
	[[Category: Catalytic triad]]		[[Category: Catalytic triad]]
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	[[Category: Neuronal ceroid lipofuscinosis]]		[[Category: Neuronal ceroid lipofuscinosis]]
	[[Category: Oxyanion hole]]		[[Category: Oxyanion hole]]
-	[[Category: Polymorphism]]
	[[Category: Prodomain]]		[[Category: Prodomain]]
	[[Category: Protease]]		[[Category: Protease]]

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

OCA — Mon, 03 Jan 2011 11:46:40 GMT

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

←Older revision

Revision as of 11:46, 3 January 2011

OCA at 11:46, 3 January 2011

OCA — Mon, 03 Jan 2011 11:46:38 GMT

←Older revision		Revision as of 11:46, 3 January 2011
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-	{{Seed}}
	[[Image:3edy.png\|left\|200px]]		[[Image:3edy.png\|left\|200px]]

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	===Crystal Structure of the Precursor Form of Human Tripeptidyl-Peptidase 1===		===Crystal Structure of the Precursor Form of Human Tripeptidyl-Peptidase 1===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_19038967}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 19038967 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_19038967}}

	==About this Structure==		==About this Structure==
-	~~3EDY is a~~ [[~~Single protein~~]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EDY OCA].	+	[[3edy]] is a 1 chain structure of [[Tripeptidyl peptidase]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EDY OCA].
		+
		+	==See Also==
		+	*[[Tripeptidyl peptidase]]
		+
		+	==Reference==
		+	<ref group="xtra">PMID:19038967</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Single protein]]
	[[Category: Tripeptidyl-peptidase I]]		[[Category: Tripeptidyl-peptidase I]]
	[[Category: Das, K.]]		[[Category: Das, K.]]
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	[[Category: Tpp1]]		[[Category: Tpp1]]
	[[Category: Zymogen]]		[[Category: Zymogen]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 20:02:34 2009''

OCA at 09:59, 18 February 2009

OCA — Wed, 18 Feb 2009 09:59:17 GMT

←Older revision		Revision as of 09:59, 18 February 2009
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	===Crystal Structure of the Precursor Form of Human Tripeptidyl-Peptidase 1===		===Crystal Structure of the Precursor Form of Human Tripeptidyl-Peptidase 1===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_19038967}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 19038967 is the PubMed ID number.
-	-->
-	{{ABSTRACT_PUBMED_19038967}}

	==About this Structure==		==About this Structure==
-	3EDY is a ~~1 chain~~ structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EDY OCA].	+	3EDY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EDY OCA].
-		+
-	~~==Reference==~~	+
-	~~<ref group="xtra">PMID:19038967</ref><references group="xtra"/>~~	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
		+	[[Category: Single protein]]
	[[Category: Tripeptidyl-peptidase I]]		[[Category: Tripeptidyl-peptidase I]]
	[[Category: Das, K.]]		[[Category: Das, K.]]
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	[[Category: Zymogen]]		[[Category: Zymogen]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed~~ Feb ~~18 08~~:42:42 2009''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 20:02:34 2009''