3ee6 - Revision history

OCA at 11:47, 16 February 2022

OCA — Wed, 16 Feb 2022 11:47:40 GMT

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

	==Crystal Structure Analysis of Tripeptidyl peptidase -I==		==Crystal Structure Analysis of Tripeptidyl peptidase -I==
-	<StructureSection load='3ee6' size='340' side='right' caption='[[3ee6]], [[Resolution\|resolution]] 2.35Å' scene=''>	+	<StructureSection load='3ee6' size='340' side='right'caption='[[3ee6]], [[Resolution\|resolution]] 2.35Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3ee6]] 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=3EE6 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3EE6 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3ee6]] is a 2 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=3EE6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EE6 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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">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">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=3ee6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ee6 OCA], [~~http~~://pdbe.org/3ee6 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3ee6 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3ee6 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3ee6 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=3ee6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ee6 OCA], [https://pdbe.org/3ee6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ee6 RCSB], [https://www.ebi.ac.uk/pdbsum/3ee6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ee6 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]]
Line 34:		Line 34:

	==See Also==		==See Also==
-	*[[Aminopeptidase\|Aminopeptidase]]
	*[[Tripeptidyl peptidase\|Tripeptidyl peptidase]]		*[[Tripeptidyl peptidase\|Tripeptidyl peptidase]]
	== References ==		== References ==
Line 41:		Line 40:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Tripeptidyl-peptidase I]]		[[Category: Tripeptidyl-peptidase I]]
	[[Category: Asif, A R]]		[[Category: Asif, A R]]

OCA at 06:05, 20 June 2018

OCA — Wed, 20 Jun 2018 06:05:24 GMT

←Older revision		Revision as of 06:05, 20 June 2018
Line 17:		Line 17:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ee/3ee6_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ee/3ee6_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>

OCA at 22:23, 5 August 2016

OCA — Fri, 05 Aug 2016 22:23:18 GMT

←Older revision		Revision as of 22:23, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal Structure Analysis of Tripeptidyl peptidase -I==		==Crystal Structure Analysis of Tripeptidyl peptidase -I==
	<StructureSection load='3ee6' size='340' side='right' caption='[[3ee6]], [[Resolution\|resolution]] 2.35Å' scene=''>		<StructureSection load='3ee6' size='340' side='right' caption='[[3ee6]], [[Resolution\|resolution]] 2.35Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3ee6]] is a 2 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=3EE6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EE6 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3ee6]] 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=3EE6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EE6 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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">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">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=3ee6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ee6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ee6 RCSB], [http://www.ebi.ac.uk/pdbsum/3ee6 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=3ee6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ee6 OCA], [http://pdbe.org/3ee6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ee6 RCSB], [http://www.ebi.ac.uk/pdbsum/3ee6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ee6 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 20:		Line 21:
	<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=3ee6 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 30:		Line 31:
	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 3ee6" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 38:		Line 40:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Tripeptidyl-peptidase I]]		[[Category: Tripeptidyl-peptidase I]]
	[[Category: Asif, A R]]		[[Category: Asif, A R]]

OCA at 13:21, 18 December 2014

OCA — Thu, 18 Dec 2014 13:21:38 GMT

←Older revision		Revision as of 13:21, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3ee6~~\| ~~PDB~~=3ee6 \| ~~SCENE~~= }}	+	==Crystal Structure Analysis of Tripeptidyl peptidase -I==
-	===~~Crystal Structure Analysis of~~ Tripeptidyl peptidase -I===	+	<StructureSection load='3ee6' size='340' side='right' caption='[[3ee6]], [[Resolution\|resolution]] 2.35Å' scene=''>
-	~~{{ABSTRACT_PUBMED_19038966}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3ee6]] is a 2 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=3EE6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EE6 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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">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=3ee6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ee6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ee6 RCSB], [http://www.ebi.ac.uk/pdbsum/3ee6 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/ee/3ee6_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, a fatal neurodegenerative disease of childhood, is caused by mutations in the TPP1 gene that encodes tripeptidyl-peptidase I. We show that purified TPP1 requires at least partial glycosylation for in vitro autoprocessing and proteolytic activity. We crystallized the fully glycosylated TPP1 precursor under conditions that implied partial autocatalytic cleavage between the prosegment and the catalytic domain. X-ray crystallographic analysis at 2.35 angstroms resolution reveals a globular structure with a subtilisin-like fold, a Ser475-Glu272-Asp360 catalytic triad, and an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases. In contrast to other S53 peptidases, the TPP1 structure revealed steric constraints on the P4 substrate pocket explaining its preferential cleavage of tripeptides from the unsubstituted N terminus of proteins. Two alternative conformations of the catalytic Asp276 are associated with the activation status of TPP1. 28 disease-causing missense mutations are analyzed in the light of the TPP1 structure providing insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis.

-	~~==Disease==~~	+	Structure of tripeptidyl-peptidase I provides insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis.,Pal A, Kraetzner R, Gruene T, Grapp M, Schreiber K, Gronborg M, Urlaub H, Becker S, Asif AR, Gartner J, Sheldrick GM, Steinfeld R J Biol Chem. 2009 Feb 6;284(6):3976-84. Epub 2008 Nov 26. PMID:19038966<ref>PMID:19038966</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==~~	+
-	~~[[3ee6]] is a 2 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=3EE6 OCA].~~	+

	==See Also==		==See Also==
		+	*[[Aminopeptidase\|Aminopeptidase]]
	*[[Tripeptidyl peptidase\|Tripeptidyl peptidase]]		*[[Tripeptidyl peptidase\|Tripeptidyl peptidase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:019038966</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Tripeptidyl-peptidase I]]		[[Category: Tripeptidyl-peptidase I]]
-	[[Category: Asif, A R.]]	+	[[Category: Asif, A R]]
-	[[Category: Becker, S.]]	+	[[Category: Becker, S]]
-	[[Category: Gartner, J.]]	+	[[Category: Gartner, J]]
-	[[Category: Granborg, M.]]	+	[[Category: Granborg, M]]
-	[[Category: Grapp, M.]]	+	[[Category: Grapp, M]]
-	[[Category: Gruene, T.]]	+	[[Category: Gruene, T]]
-	[[Category: Kraetzner, R.]]	+	[[Category: Kraetzner, R]]
-	[[Category: Pal, A.]]	+	[[Category: Pal, A]]
-	[[Category: Schreiber, K.]]	+	[[Category: Schreiber, K]]
-	[[Category: Sheldrick, G M.]]	+	[[Category: Sheldrick, G M]]
-	[[Category: Steinfeld, R.]]	+	[[Category: Steinfeld, R]]
-	[[Category: Urlaub, H.]]	+	[[Category: Urlaub, H]]
	[[Category: Disease mutation]]		[[Category: Disease mutation]]
	[[Category: Epilepsy]]		[[Category: Epilepsy]]

OCA at 06:29, 25 March 2013

OCA — Mon, 25 Mar 2013 06:29:26 GMT

←Older revision		Revision as of 06:29, 25 March 2013
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-	[[Image:3ee6.png\|left\|200px]]
-
	{{STRUCTURE_3ee6\| PDB=3ee6 \| SCENE= }}		{{STRUCTURE_3ee6\| PDB=3ee6 \| SCENE= }}
-
	===Crystal Structure Analysis of Tripeptidyl peptidase -I===		===Crystal Structure Analysis of Tripeptidyl peptidase -I===
		+	{{ABSTRACT_PUBMED_19038966}}

-	~~{{ABSTRACT_PUBMED_19038966}}~~	+	==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:019038966</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019038966</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Tripeptidyl-peptidase I]]		[[Category: Tripeptidyl-peptidase I]]

OCA at 22:22, 20 October 2012

OCA — Sat, 20 Oct 2012 22:22:13 GMT

←Older revision		Revision as of 22:22, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3ee6]] is a 2 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=3EE6 OCA].	+	[[3ee6]] is a 2 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=3EE6 OCA].

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

OCA at 16:04, 27 July 2012

OCA — Fri, 27 Jul 2012 16:04:12 GMT

←Older revision		Revision as of 16:04, 27 July 2012
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	[[Image:3ee6.png\|left\|200px]]		[[Image:3ee6.png\|left\|200px]]

-	<!--
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-	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_3ee6\| PDB=3ee6 \| SCENE= }}		{{STRUCTURE_3ee6\| PDB=3ee6 \| SCENE= }}

	===Crystal Structure Analysis of Tripeptidyl peptidase -I===		===Crystal Structure Analysis of Tripeptidyl peptidase -I===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_19038966}}, adds the Publication Abstract to the page
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	{{ABSTRACT_PUBMED_19038966}}		{{ABSTRACT_PUBMED_19038966}}

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

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~19038966~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019038966</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Tripeptidyl-peptidase I]]		[[Category: Tripeptidyl-peptidase I]]
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	[[Category: Steinfeld, R.]]		[[Category: Steinfeld, R.]]
	[[Category: Urlaub, H.]]		[[Category: Urlaub, H.]]
-	[[Category: Alternative splicing]]
	[[Category: Disease mutation]]		[[Category: Disease mutation]]
	[[Category: Epilepsy]]		[[Category: Epilepsy]]
Line 47:		Line 35:
	[[Category: Lysosome]]		[[Category: Lysosome]]
	[[Category: Neuronal ceroid lipofuscinosis]]		[[Category: Neuronal ceroid lipofuscinosis]]
-	[[Category: Polymorphism]]
	[[Category: Protease]]		[[Category: Protease]]
	[[Category: Serine protease]]		[[Category: Serine protease]]
	[[Category: Tripepetidyl peptidase -i]]		[[Category: Tripepetidyl peptidase -i]]
	[[Category: Zymogen]]		[[Category: Zymogen]]

OCA: Protected "3ee6" [edit=sysop:move=sysop]

OCA — Mon, 03 Jan 2011 11:47:04 GMT

Protected "3ee6" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:47, 3 January 2011

OCA at 11:47, 3 January 2011

OCA — Mon, 03 Jan 2011 11:47:03 GMT

←Older revision		Revision as of 11:47, 3 January 2011
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-	{{Seed}}
	[[Image:3ee6.png\|left\|200px]]		[[Image:3ee6.png\|left\|200px]]

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	-->		-->
	{{ABSTRACT_PUBMED_19038966}}		{{ABSTRACT_PUBMED_19038966}}
-
-	==Disease==
-	Known disease associated with this structure: Ceroid-lipofuscinosis, neuronal 2, classic late infantile OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=607998 607998]]

	==About this Structure==		==About this Structure==
-	~~3EE6~~ is a 2 ~~chains~~ structure of ~~sequences~~ 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=3EE6 OCA].	+	[[3ee6]] is a 2 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=3EE6 OCA].
		+
		+	==See Also==
		+	*[[Tripeptidyl peptidase]]

	==Reference==		==Reference==
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	[[Category: Tripepetidyl peptidase -i]]		[[Category: Tripepetidyl peptidase -i]]
	[[Category: Zymogen]]		[[Category: Zymogen]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 27 14:26:13 2009''

OCA at 11:26, 27 May 2009

OCA — Wed, 27 May 2009 11:26:13 GMT

←Older revision		Revision as of 11:26, 27 May 2009
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	{{Seed}}		{{Seed}}
-	[[Image:3ee6.~~jpg~~\|left\|200px]]	+	[[Image:3ee6.png\|left\|200px]]

	<!--		<!--
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	===Crystal Structure Analysis of Tripeptidyl peptidase -I===		===Crystal Structure Analysis of Tripeptidyl peptidase -I===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_19038966}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 19038966 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_19038966}}

	==Disease==		==Disease==
Line 18:		Line 24:
	==About this Structure==		==About this Structure==
	3EE6 is a 2 chains structure of sequences 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=3EE6 OCA].		3EE6 is a 2 chains structure of sequences 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=3EE6 OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:19038966</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Tripeptidyl-peptidase I]]		[[Category: Tripeptidyl-peptidase I]]
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	[[Category: Zymogen]]		[[Category: Zymogen]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Thu Nov~~ 27 13:39:~~18 2008~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 27 14:26:13 2009''