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New page: left|200px<br /> <applet load="1czy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1czy, resolution 2.00Å" /> '''CRYSTAL STRUCTURE O...
 
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[[Image:1czy.gif|left|200px]]<br />
<applet load="1czy" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1czy, resolution 2.00&Aring;" />
'''CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE TRAF DOMAIN OF HUMAN TRAF2 AND AN LMP1 BINDING PEPTIDE'''<br />


==Overview==
==CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE TRAF DOMAIN OF HUMAN TRAF2 AND AN LMP1 BINDING PEPTIDE==
Many members of the tumor necrosis factor receptor (TNFR) superfamily, initiate intracellular signaling by recruiting TNFR-associated factors, (TRAFs) through their cytoplasmic tails. TRAFs apparently recognize highly, diverse receptor sequences. Crystal structures of the TRAF domain of human, TRAF2 in complex with peptides from the TNFR family members CD40, CD30, Ox40, 4-1BB, and the EBV oncoprotein LMP1 revealed a conserved binding, mode. A major TRAF2-binding consensus sequence, (P/S/A/T)x(Q/E)E, and a, minor consensus motif, PxQxxD, can be defined from the structural, analysis, which encompass all known TRAF2-binding sequences. The, structural information provides a template for the further dissection of, receptor binding specificity of TRAF2 and for the understanding of the, complexity of TRAF-mediated signal transduction.
<StructureSection load='1czy' size='340' side='right'caption='[[1czy]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1czy]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_herpesvirus_4_strain_B95-8 Human herpesvirus 4 strain B95-8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CZY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CZY 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=ACE:ACETYL+GROUP'>ACE</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=1czy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1czy OCA], [https://pdbe.org/1czy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1czy RCSB], [https://www.ebi.ac.uk/pdbsum/1czy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1czy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LMP1_EBVB9 LMP1_EBVB9] Acts as a CD40 functional homolog to prevent apoptosis of infected B-lymphocytes and drive their proliferation. Functions as a constitutively active tumor necrosis factor receptor that induces the activation of several signaling pathways, including those of the nuclear factor-kappa-B family. LMP1 signaling leads to up-regulation of antiapoptotic proteins and provide growth signals in latently infected cells. It is a short-lived protein probably degraded by the proteasome.
== 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/cz/1czy_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1czy ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Many members of the tumor necrosis factor receptor (TNFR) superfamily initiate intracellular signaling by recruiting TNFR-associated factors (TRAFs) through their cytoplasmic tails. TRAFs apparently recognize highly diverse receptor sequences. Crystal structures of the TRAF domain of human TRAF2 in complex with peptides from the TNFR family members CD40, CD30, Ox40, 4-1BB, and the EBV oncoprotein LMP1 revealed a conserved binding mode. A major TRAF2-binding consensus sequence, (P/S/A/T)x(Q/E)E, and a minor consensus motif, PxQxxD, can be defined from the structural analysis, which encompass all known TRAF2-binding sequences. The structural information provides a template for the further dissection of receptor binding specificity of TRAF2 and for the understanding of the complexity of TRAF-mediated signal transduction.


==About this Structure==
The structural basis for the recognition of diverse receptor sequences by TRAF2.,Ye H, Park YC, Kreishman M, Kieff E, Wu H Mol Cell. 1999 Sep;4(3):321-30. PMID:10518213<ref>PMID:10518213</ref>
1CZY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ACE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CZY OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
The structural basis for the recognition of diverse receptor sequences by TRAF2., Ye H, Park YC, Kreishman M, Kieff E, Wu H, Mol Cell. 1999 Sep;4(3):321-30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10518213 10518213]
</div>
<div class="pdbe-citations 1czy" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[TNF receptor-associated factor 3D structures|TNF receptor-associated factor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Human herpesvirus 4 strain B95-8]]
[[Category: Kieff, E.]]
[[Category: Large Structures]]
[[Category: Kreishman, M.]]
[[Category: Kieff E]]
[[Category: Park, Y.C.]]
[[Category: Kreishman M]]
[[Category: Wu, H.]]
[[Category: Park YC]]
[[Category: Ye, H.]]
[[Category: Wu H]]
[[Category: ACE]]
[[Category: Ye H]]
[[Category: beta sandwich]]
[[Category: protein-peptide complex]]
[[Category: signaling protein]]
 
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