5xme

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==Solution structure of C-terminal domain of TRADD==
==Solution structure of C-terminal domain of TRADD==
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<StructureSection load='5xme' size='340' side='right' caption='[[5xme]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
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<StructureSection load='5xme' size='340' side='right'caption='[[5xme]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5xme]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XME OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XME FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5xme]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XME OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XME FirstGlance]. <br>
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</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=5xme FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xme OCA], [http://pdbe.org/5xme PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xme RCSB], [http://www.ebi.ac.uk/pdbsum/5xme PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xme ProSAT]</span></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">Solution NMR</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=5xme FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xme OCA], [https://pdbe.org/5xme PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xme RCSB], [https://www.ebi.ac.uk/pdbsum/5xme PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xme ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/TRADD_HUMAN TRADD_HUMAN]] The nuclear form acts as a tumor suppressor by preventing ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A by TRIP12: acts by interacting with TRIP12, leading to disrupt interaction between TRIP12 and isoform p19ARF/ARF of CDKN2A (By similarity). Adapter molecule for TNFRSF1A/TNFR1 that specifically associates with the cytoplasmic domain of activated TNFRSF1A/TNFR1 mediating its interaction with FADD. Overexpression of TRADD leads to two major TNF-induced responses, apoptosis and activation of NF-kappa-B.
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[https://www.uniprot.org/uniprot/TRADD_HUMAN TRADD_HUMAN] The nuclear form acts as a tumor suppressor by preventing ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A by TRIP12: acts by interacting with TRIP12, leading to disrupt interaction between TRIP12 and isoform p19ARF/ARF of CDKN2A (By similarity). Adapter molecule for TNFRSF1A/TNFR1 that specifically associates with the cytoplasmic domain of activated TNFRSF1A/TNFR1 mediating its interaction with FADD. Overexpression of TRADD leads to two major TNF-induced responses, apoptosis and activation of NF-kappa-B.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The TNFR1-associated death domain protein (TRADD) is an intracellular adaptor protein involved in various signaling pathways, such as antiapoptosis. Its C-terminal death domain (DD) is responsible for binding other DD-containing proteins including the p75 neurotrophin receptor (p75NTR). Here we present a solution structure of TRADD DD derived from high-resolution NMR spectroscopy. The TRADD DD comprises two super-secondary structures, an all-helix Greek key motif and a beta-hairpin motif flanked by two alpha helices, which make it unique among all known DD structures. The beta-hairpin motif is essential for TRADD DD to fold into a functional globular domain. The highly-charged surface suggests a critical role of electrostatic interactions in TRADD DD-mediated signaling. This novel structure represents a new class within the DD superfamily and provides a structural basis for studying homotypic DD interactions. NMR titration revealed a direct weak interaction between TRADD DD and p75NTR DD monomers. A binding site next to the p75NTR DD homodimerization interface indicates that TRADD DD recruitment to p75NTR requires separation of the p75NTR DD homodimer, explaining the mechanism of NGF-dependent activation of p75NTR-TRADD-mediated antiapoptotic pathway in breast cancer cell.
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Structure of the C-terminal domain of TRADD reveals a novel fold in the death domain superfamily.,Zhang N, Yuan W, Fan JS, Lin Z Sci Rep. 2017 Aug 1;7(1):7073. doi: 10.1038/s41598-017-07348-9. PMID:28765645<ref>PMID:28765645</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5xme" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Lin, Z]]
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[[Category: Homo sapiens]]
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[[Category: Zhang, N]]
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[[Category: Large Structures]]
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[[Category: Apoptosis]]
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[[Category: Lin Z]]
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[[Category: Death domain]]
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[[Category: Zhang N]]
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[[Category: Tradd]]
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Current revision

Solution structure of C-terminal domain of TRADD

PDB ID 5xme

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