1f3v: Difference between revisions

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[[Image:1f3v.gif|left|200px]]<br /><applet load="1f3v" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1f3v, resolution 2.0&Aring;" />
'''CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE N-TERMINAL DOMAIN OF TRADD AND THE TRAF DOMAIN OF TRAF2'''<br />


==Overview==
==Crystal structure of the complex between the N-terminal domain of TRADD and the TRAF domain of TRAF2==
TRAF proteins are major mediators for the cell activation, cell survival, and antiapoptotic functions of the TNF receptor superfamily. They can be recruited to activated TNF receptors either by direct interactions with the receptors or indirectly via the adaptor protein TRADD. We now report the structure of the TRADD-TRAF2 complex, which is highly distinct from receptor-TRAF2 interactions. This interaction is significantly stronger and we show by an in vivo signaling assay that TRAF2 signaling is more readily initiated by TRADD than by direct receptor-TRAF2 interactions. TRADD is specific for TRAF1 and TRAF2, which ensures the recruitment of clAPs for the direct inhibition of caspase activation in the signaling complex. The stronger affinity and unique specificity of the TRADD-TRAF2 interaction are crucial for the suppression of apoptosis and provide a mechanistic basis for the perturbation of TRAF recruitment in sensitizing cell death induction.
<StructureSection load='1f3v' size='340' side='right'caption='[[1f3v]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1f3v]] 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=1F3V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F3V FirstGlance]. <br>
</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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1f3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f3v OCA], [https://pdbe.org/1f3v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f3v RCSB], [https://www.ebi.ac.uk/pdbsum/1f3v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f3v ProSAT]</span></td></tr>
</table>
== Function ==
[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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f3/1f3v_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1f3v ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1F3V is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F3V OCA].
*[[TNF receptor-associated factor|TNF receptor-associated factor]]
 
*[[TNF receptor-associated factor 3D structures|TNF receptor-associated factor 3D structures]]
==Reference==
__TOC__
A novel mechanism of TRAF signaling revealed by structural and functional analyses of the TRADD-TRAF2 interaction., Park YC, Ye H, Hsia C, Segal D, Rich RL, Liou HC, Myszka DG, Wu H, Cell. 2000 Jun 23;101(7):777-87. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10892748 10892748]
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Hsia, C.]]
[[Category: Hsia C]]
[[Category: Liou, H C.]]
[[Category: Liou H-C]]
[[Category: Myszka, D.]]
[[Category: Myszka D]]
[[Category: Park, Y C.]]
[[Category: Park YC]]
[[Category: Rich, R.]]
[[Category: Rich R]]
[[Category: Segal, D.]]
[[Category: Segal D]]
[[Category: Wu, H.]]
[[Category: Wu H]]
[[Category: Ye, H.]]
[[Category: Ye H]]
[[Category: a-b sandwich]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:34:34 2008''

Latest revision as of 13:09, 20 March 2024

Crystal structure of the complex between the N-terminal domain of TRADD and the TRAF domain of TRAF2Crystal structure of the complex between the N-terminal domain of TRADD and the TRAF domain of TRAF2

Structural highlights

1f3v is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:
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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1f3v, resolution 2.00Å

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