3n3k: Difference between revisions

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==The catalytic domain of USP8 in complex with a USP8 specific inhibitor==
==The catalytic domain of USP8 in complex with a USP8 specific inhibitor==
<StructureSection load='3n3k' size='340' side='right' caption='[[3n3k]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='3n3k' size='340' side='right'caption='[[3n3k]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3n3k]] 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=3N3K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3N3K FirstGlance]. <br>
<table><tr><td colspan='2'>[[3n3k]] 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=3N3K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3N3K FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.6&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2gfo|2gfo]], [[2a9u|2a9u]], [[1whb|1whb]], [[2fzp|2fzp]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KIAA0055, UBPY, USP8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), RPS27A, UBA52, UBA80, UBB, UBC, UBCEP1, UBCEP2, UBQ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3n3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n3k OCA], [https://pdbe.org/3n3k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3n3k RCSB], [https://www.ebi.ac.uk/pdbsum/3n3k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3n3k ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitin_thiolesterase Ubiquitin thiolesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.15 3.1.2.15] </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=3n3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n3k OCA], [http://pdbe.org/3n3k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3n3k RCSB], [http://www.ebi.ac.uk/pdbsum/3n3k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3n3k ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/UBP8_HUMAN UBP8_HUMAN]] Hydrolase that can remove conjugated ubiquitin from proteins and therefore plays an important regulatory role at the level of protein turnover by preventing degradation. Converts both 'Lys-48' an 'Lys-63'-linked ubiquitin chains. Catalytic activity is enhanced in the M phase. Involved in cell proliferation. Required to enter into S phase in response to serum stimulation. May regulate T-cell anergy mediated by RNF128 via the formation of a complex containing RNF128 and OTUB1. Probably regulates the stability of STAM2 and RASGRF1. Regulates endosomal ubiquitin dynamics, cargo sorting, membrane traffic at early endosomes, and maintenance of ESCRT-0 stability. The level of protein ubiquitination on endosomes is essential for maintaining the morphology of the organelle. Deubiquitinates EPS15 and controles tyrosine kinase stability. Removes conjugated ubiquitin from EGFR thus regulating EGFR degradation and downstream MAPK signaling. Involved in acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules. Deubiquitinates BIRC6/bruce and KIF23/MKLP1.<ref>PMID:9628861</ref> <ref>PMID:16520378</ref> <ref>PMID:17711858</ref> <ref>PMID:18329369</ref>
[https://www.uniprot.org/uniprot/UBP8_HUMAN UBP8_HUMAN] Hydrolase that can remove conjugated ubiquitin from proteins and therefore plays an important regulatory role at the level of protein turnover by preventing degradation. Converts both 'Lys-48' an 'Lys-63'-linked ubiquitin chains. Catalytic activity is enhanced in the M phase. Involved in cell proliferation. Required to enter into S phase in response to serum stimulation. May regulate T-cell anergy mediated by RNF128 via the formation of a complex containing RNF128 and OTUB1. Probably regulates the stability of STAM2 and RASGRF1. Regulates endosomal ubiquitin dynamics, cargo sorting, membrane traffic at early endosomes, and maintenance of ESCRT-0 stability. The level of protein ubiquitination on endosomes is essential for maintaining the morphology of the organelle. Deubiquitinates EPS15 and controles tyrosine kinase stability. Removes conjugated ubiquitin from EGFR thus regulating EGFR degradation and downstream MAPK signaling. Involved in acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules. Deubiquitinates BIRC6/bruce and KIF23/MKLP1.<ref>PMID:9628861</ref> <ref>PMID:16520378</ref> <ref>PMID:17711858</ref> <ref>PMID:18329369</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==See Also==
==See Also==
*[[Thioesterase|Thioesterase]]
*[[Thioesterase 3D structures|Thioesterase 3D structures]]
*[[Ubiquitin|Ubiquitin]]
*[[3D structures of ubiquitin|3D structures of ubiquitin]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Ubiquitin thiolesterase]]
[[Category: Large Structures]]
[[Category: Allali-Hassani, A]]
[[Category: Allali-Hassani A]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith CH]]
[[Category: Avvakumov, G V]]
[[Category: Avvakumov GV]]
[[Category: Bochkarev, A]]
[[Category: Bochkarev A]]
[[Category: Bountra, C]]
[[Category: Bountra C]]
[[Category: Dhe-Paganon S]]
[[Category: Edwards AM]]
[[Category: Ernst A]]
[[Category: Lam R]]
[[Category: Li Y]]
[[Category: Sidhu S]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: Dhe-Paganon, S]]
[[Category: Walker JR]]
[[Category: Edwards, A M]]
[[Category: Weigelt J]]
[[Category: Ernst, A]]
[[Category: Xue S]]
[[Category: Lam, R]]
[[Category: Li, Y]]
[[Category: Sidhu, S]]
[[Category: Walker, J R]]
[[Category: Weigelt, J]]
[[Category: Xue, S]]
[[Category: Deubiquitinating enzyme]]
[[Category: Dub]]
[[Category: Hydrolase]]
[[Category: Inhibitor]]
[[Category: Isopeptide bond]]
[[Category: Nucleus]]
[[Category: Phosphoprotein]]
[[Category: Protease]]
[[Category: Sgc]]
[[Category: Thiol protease]]
[[Category: Ubiquitin]]
[[Category: Ubl conjugation pathway]]
[[Category: Zinc ribbon]]

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