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5dws

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==Crystal Structure of ITCH WW3 domain in complex with TXNIP peptide==
==Crystal Structure of ITCH WW3 domain in complex with TXNIP peptide==
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<StructureSection load='5dws' size='340' side='right' caption='[[5dws]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
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<StructureSection load='5dws' size='340' side='right'caption='[[5dws]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5dws]] is a 8 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4rre 4rre]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DWS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DWS FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5dws]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4rre 4rre]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DWS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DWS FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
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<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=5dws FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dws OCA], [http://pdbe.org/5dws PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dws RCSB], [http://www.ebi.ac.uk/pdbsum/5dws PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5dws FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dws OCA], [https://pdbe.org/5dws PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dws RCSB], [https://www.ebi.ac.uk/pdbsum/5dws PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dws ProSAT]</span></td></tr>
</table>
</table>
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== Disease ==
 
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[[http://www.uniprot.org/uniprot/ITCH_HUMAN ITCH_HUMAN]] Defects in ITCH are the cause of syndromic multisystem autoimmune disease (SMAD) [MIM:[http://omim.org/entry/613385 613385]]. SMAD is characterized by organomegaly, failure to thrive, developmental delay, dysmorphic features and autoimmune inflammatory cell infiltration of the lungs, liver and gut.<ref>PMID:20170897</ref>
 
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ITCH_HUMAN ITCH_HUMAN]] Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. It catalyzes 'Lys-29'-, 'Lys-48'- and 'Lys-63'-linked ubiquitin conjugation. It is involved in the control of inflammatory signaling pathways. Is an essential component of a ubiquitin-editing protein complex, comprising also TNFAIP3, TAX1BP1 and RNF11, that ensures the transient nature of inflammatory signaling pathways. Promotes the association of the complex after TNF stimulation. Once the complex is formed, TNFAIP3 deubiquitinates 'Lys-63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NFKB1. Ubiquitinates RIPK2 by 'Lys-63'-linked conjugation and influences NOD2-dependent signal transduction pathways. Regulates the transcriptional activity of several transcription factors, and probably plays an important role in the regulation of immune response. Ubiquitinates NFE2 by 'Lys-63' linkages and is implicated in the control of the development of hematopoietic lineages. Critical regulator of T-helper (TH2) cytokine development through its ability to induce JUNB ubiquitination and degradation (By similarity). Ubiquitinates SNX9. Ubiquitinates CXCR4 and HGS/HRS and regulates sorting of CXCR4 to the degradative pathway. It is involved in the negative regulation of MAVS-dependent cellular antiviral responses. Ubiquitinates MAVS through 'Lys-48'-linked conjugation resulting in MAVS proteasomal degradation. Involved in the regulation of apoptosis and reactive oxygen species levels through the ubiquitination and proteasomal degradation of TXNIP. Mediates the antiapoptotic activity of epidermal growth factor through the ubiquitination and proteasomal degradation of p15 BID. Targets DTX1 for lysosomal degradation and controls NOTCH1 degradation, in the absence of ligand, through 'Lys-29'-linked polyubiquitination.<ref>PMID:14602072</ref> <ref>PMID:17028573</ref> <ref>PMID:16387660</ref> <ref>PMID:18718448</ref> <ref>PMID:18718449</ref> <ref>PMID:18628966</ref> <ref>PMID:19592251</ref> <ref>PMID:19131965</ref> <ref>PMID:19881509</ref> <ref>PMID:20392206</ref> <ref>PMID:20068034</ref>
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[https://www.uniprot.org/uniprot/TXNIP_HUMAN TXNIP_HUMAN] May act as an oxidative stress mediator by inhibiting thioredoxin activity or by limiting its bioavailability. Interacts with COPS5 and restores COPS5-induced suppression of CDKN1B stability, blocking the COPS5-mediated translocation of CDKN1B from the nucleus to the cytoplasm. Functions as a transcriptional repressor, possibly by acting as a bridge molecule between transcription factors and corepressor complexes, and over-expression will induce G0/G1 cell cycle arrest. Required for the maturation of natural killer cells. Acts as a suppressor of tumor cell growth. Inhibits the proteasomal degradation of DDIT4, and thereby contributes to the inhibition of the mammalian target of rapamycin complex 1 (mTORC1).<ref>PMID:17603038</ref> <ref>PMID:12821938</ref> <ref>PMID:18541147</ref> <ref>PMID:21460850</ref>
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==See Also==
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*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Arrowsmith, C H]]
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[[Category: Homo sapiens]]
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[[Category: Bountra, C]]
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[[Category: Large Structures]]
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[[Category: Dong, A]]
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[[Category: Arrowsmith CH]]
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[[Category: Edwards, A M]]
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[[Category: Bountra C]]
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[[Category: Liu, Y]]
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[[Category: Dong A]]
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[[Category: Min, J]]
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[[Category: Edwards AM]]
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[[Category: Structural genomic]]
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[[Category: Liu Y]]
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[[Category: Tempel, W]]
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[[Category: Min J]]
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[[Category: Ligase]]
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[[Category: Tempel W]]
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[[Category: Sgc]]
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Current revision

Crystal Structure of ITCH WW3 domain in complex with TXNIP peptide

PDB ID 5dws

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