We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

5dod

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 5dod is ON HOLD until Paper Publication
+
==Human A20 OTU domain with I325N and alkylated C103 to 2.5A resolution==
-
 
+
<StructureSection load='5dod' size='340' side='right' caption='[[5dod]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
-
Authors: Langley, D.B., Christ, D., Grey, S.T.
+
== Structural highlights ==
-
 
+
<table><tr><td colspan='2'>[[5dod]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DOD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DOD FirstGlance]. <br>
-
Description: Human A20 OTU domain with I325N and alkylated C103 to 2.5A resolution
+
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=YCM:S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE'>YCM</scene></td></tr>
-
[[Category: Unreleased Structures]]
+
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4zrh|4zrh]]</td></tr>
-
[[Category: Langley, D.B]]
+
<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=5dod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dod OCA], [http://pdbe.org/5dod PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dod RCSB], [http://www.ebi.ac.uk/pdbsum/5dod PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dod ProSAT]</span></td></tr>
-
[[Category: Grey, S.T]]
+
</table>
 +
== Function ==
 +
[[http://www.uniprot.org/uniprot/TNAP3_HUMAN TNAP3_HUMAN]] Ubiquitin-editing enzyme that contains both ubiquitin ligase and deubiquitinase activities. Involved in immune and inflammatory responses signaled by cytokines, such as TNF-alpha and IL-1 beta, or pathogens via Toll-like receptors (TLRs) through terminating NF-kappa-B activity. Essential component of a ubiquitin-editing protein complex, comprising also RNF11, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. In cooperation with TAX1BP1 promotes disassembly of E2-E3 ubiquitin protein ligase complexes in IL-1R and TNFR-1 pathways; affected are at least E3 ligases TRAF6, TRAF2 and BIRC2, and E2 ubiquitin-conjugating enzymes UBE2N and UBE2D3. In cooperation with TAX1BP1 promotes ubiquitination of UBE2N and proteasomal degradation of UBE2N and UBE2D3. Upon TNF stimulation, 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 NF-kappa-B. Deubiquinates TRAF6 probably acting on 'Lys-63'-linked polyubiquitin. Upon T-cell receptor (TCR)-mediated T-cell activation, deubiquitinates 'Lys-63'-polyubiquitin chains on MALT1 thereby mediating disassociation of the CBM (CARD11:BCL10:MALT1) and IKK complexes and preventing sustained IKK activation. Deubiquinates NEMO/IKBKG; the function is facilitated by TNIP1 and leads to inhibition of NF-kappa-B activation. Upon stimulation by bacterial peptidoglycans, probably deubiquitinates RIPK2. Can also inhibit I-kappa-B-kinase (IKK) through a non-catalytic mechanism which involves polyubiquitin; polyubiquitin promotes association with IKBKG and prevents IKK MAP3K7-mediated phosphorylation. Targets TRAF2 for lysosomal degradation. In vitro able to deubiquitinate both 'Lys-48'- and 'Lys-63' polyubiquitin chains. Inhibitor of programmed cell death. Has a role in the function of the lymphoid system.<ref>PMID:8692885</ref> <ref>PMID:9299557</ref> <ref>PMID:9882303</ref> <ref>PMID:14748687</ref> <ref>PMID:15258597</ref> <ref>PMID:16684768</ref> <ref>PMID:18952128</ref> <ref>PMID:19494296</ref> <ref>PMID:22099304</ref> <ref>PMID:17961127</ref> <ref>PMID:18164316</ref>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Christ, D]]
[[Category: Christ, D]]
 +
[[Category: Grey, S T]]
 +
[[Category: Langley, D B]]
 +
[[Category: Hydrolase]]
 +
[[Category: Ubiquitin protease]]

Revision as of 13:46, 21 September 2016

Human A20 OTU domain with I325N and alkylated C103 to 2.5A resolution

5dod, resolution 2.50Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools