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5xme

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Revision as of 06:54, 14 October 2020

Solution structure of C-terminal domain of TRADD

Structural highlights

5xme is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Zhang N, Yuan W, Fan JS, Lin Z. Structure of the C-terminal domain of TRADD reveals a novel fold in the death domain superfamily. Sci Rep. 2017 Aug 1;7(1):7073. doi: 10.1038/s41598-017-07348-9. PMID:28765645 doi:http://dx.doi.org/10.1038/s41598-017-07348-9

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5xme"

@@ Line 1: / Line 1: @@
 ==Solution structure of C-terminal domain of TRADD==
-<StructureSection load='5xme' size='340' side='right' caption='[[5xme]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
+<StructureSection load='5xme' size='340' side='right'caption='[[5xme]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
 == Structural highlights ==
-<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>
+<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://proteopedia.org/fgij/fg.htm?mol=5XME FirstGlance]. <br>
-</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>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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>
 </table>
 == Function ==
@@ Line 21: / Line 21: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Lin, Z]]
 [[Category: Zhang, N]]

5xme

From Proteopedia

Revision as of 06:54, 14 October 2020

Solution structure of C-terminal domain of TRADD

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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