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| | <StructureSection load='3gro' size='340' side='right'caption='[[3gro]], [[Resolution|resolution]] 2.53Å' scene=''> | | <StructureSection load='3gro' size='340' side='right'caption='[[3gro]], [[Resolution|resolution]] 2.53Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3gro]] 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=3GRO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GRO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3gro]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GRO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GRO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.53Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPT1, PPT ([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'>[https://en.wikipedia.org/wiki/Palmitoyl-protein_hydrolase Palmitoyl-protein hydrolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.22 3.1.2.22] </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=3gro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gro OCA], [https://pdbe.org/3gro PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gro RCSB], [https://www.ebi.ac.uk/pdbsum/3gro PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gro 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=3gro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gro OCA], [https://pdbe.org/3gro PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gro RCSB], [https://www.ebi.ac.uk/pdbsum/3gro PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gro ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[https://www.uniprot.org/uniprot/PPT1_HUMAN PPT1_HUMAN]] CLN1 disease. The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:7637805</ref> <ref>PMID:9425237</ref> <ref>PMID:9664077</ref> <ref>PMID:11506414</ref> <ref>PMID:19201763</ref> <ref>PMID:21990111</ref>
| + | [https://www.uniprot.org/uniprot/PPT1_HUMAN PPT1_HUMAN] CLN1 disease. The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:7637805</ref> <ref>PMID:9425237</ref> <ref>PMID:9664077</ref> <ref>PMID:11506414</ref> <ref>PMID:19201763</ref> <ref>PMID:21990111</ref> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PPT1_HUMAN PPT1_HUMAN]] Removes thioester-linked fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides during lysosomal degradation. Prefers acyl chain lengths of 14 to 18 carbons.
| + | [https://www.uniprot.org/uniprot/PPT1_HUMAN PPT1_HUMAN] Removes thioester-linked fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides during lysosomal degradation. Prefers acyl chain lengths of 14 to 18 carbons. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Palmitoyl-protein hydrolase]]
| + | [[Category: Arrowsmith CH]] |
| - | [[Category: Arrowsmith, C H]] | + | [[Category: Bochkarev A]] |
| - | [[Category: Bochkarev, A]] | + | [[Category: Bountra C]] |
| - | [[Category: Bountra, C]] | + | [[Category: Cossar D]] |
| - | [[Category: Cossar, D]] | + | [[Category: Dobrovetsky E]] |
| - | [[Category: Dobrovetsky, E]] | + | [[Category: Dong A]] |
| - | [[Category: Dong, A]] | + | [[Category: Edwards AM]] |
| - | [[Category: Edwards, A M]] | + | [[Category: Park H]] |
| - | [[Category: Park, H]] | + | [[Category: Seitova A]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Tempel W]] |
| - | [[Category: Seitova, A]] | + | [[Category: Tong Y]] |
| - | [[Category: Tempel, W]] | + | [[Category: Weigelt J]] |
| - | [[Category: Tong, Y]] | + | |
| - | [[Category: Weigelt, J]] | + | |
| - | [[Category: Disease mutation]]
| + | |
| - | [[Category: Disulfide bond]]
| + | |
| - | [[Category: Glycoprotein]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Lysosome]]
| + | |
| - | [[Category: Neurodegeneration]]
| + | |
| - | [[Category: Neuronal ceroid lipofuscinosis]]
| + | |
| - | [[Category: Polymorphism]]
| + | |
| - | [[Category: Sensory transduction]]
| + | |
| - | [[Category: Sgc]]
| + | |
| - | [[Category: Vision]]
| + | |
| Structural highlights
Disease
PPT1_HUMAN CLN1 disease. The disease is caused by mutations affecting the gene represented in this entry.[1] [2] [3] [4] [5] [6]
Function
PPT1_HUMAN Removes thioester-linked fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides during lysosomal degradation. Prefers acyl chain lengths of 14 to 18 carbons.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
See Also
References
- ↑ Vesa J, Hellsten E, Verkruyse LA, Camp LA, Rapola J, Santavuori P, Hofmann SL, Peltonen L. Mutations in the palmitoyl protein thioesterase gene causing infantile neuronal ceroid lipofuscinosis. Nature. 1995 Aug 17;376(6541):584-7. PMID:7637805 doi:http://dx.doi.org/10.1038/376584a0
- ↑ Mitchison HM, Hofmann SL, Becerra CH, Munroe PB, Lake BD, Crow YJ, Stephenson JB, Williams RE, Hofman IL, Taschner PE, Martin JJ, Philippart M, Andermann E, Andermann F, Mole SE, Gardiner RM, O'Rawe AM. Mutations in the palmitoyl-protein thioesterase gene (PPT; CLN1) causing juvenile neuronal ceroid lipofuscinosis with granular osmiophilic deposits. Hum Mol Genet. 1998 Feb;7(2):291-7. PMID:9425237
- ↑ Das AK, Becerra CH, Yi W, Lu JY, Siakotos AN, Wisniewski KE, Hofmann SL. Molecular genetics of palmitoyl-protein thioesterase deficiency in the U.S. J Clin Invest. 1998 Jul 15;102(2):361-70. PMID:9664077 doi:http://dx.doi.org/10.1172/JCI3112
- ↑ van Diggelen OP, Thobois S, Tilikete C, Zabot MT, Keulemans JL, van Bunderen PA, Taschner PE, Losekoot M, Voznyi YV. Adult neuronal ceroid lipofuscinosis with palmitoyl-protein thioesterase deficiency: first adult-onset patients of a childhood disease. Ann Neurol. 2001 Aug;50(2):269-72. PMID:11506414
- ↑ Kousi M, Siintola E, Dvorakova L, Vlaskova H, Turnbull J, Topcu M, Yuksel D, Gokben S, Minassian BA, Elleder M, Mole SE, Lehesjoki AE. Mutations in CLN7/MFSD8 are a common cause of variant late-infantile neuronal ceroid lipofuscinosis. Brain. 2009 Mar;132(Pt 3):810-9. doi: 10.1093/brain/awn366. Epub 2009 Feb 5. PMID:19201763 doi:10.1093/brain/awn366
- ↑ Kousi M, Lehesjoki AE, Mole SE. Update of the mutation spectrum and clinical correlations of over 360 mutations in eight genes that underlie the neuronal ceroid lipofuscinoses. Hum Mutat. 2012 Jan;33(1):42-63. doi: 10.1002/humu.21624. Epub 2011 Nov 16. PMID:21990111 doi:10.1002/humu.21624
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