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[[Image:2hac.jpg|left|200px]]


{{Structure
==Structure of Zeta-Zeta Transmembrane Dimer==
|PDB= 2hac |SIZE=350|CAPTION= <scene name='initialview01'>2hac</scene>
<StructureSection load='2hac' size='340' side='right'caption='[[2hac]]' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[2hac]] is a 2 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=2HAC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HAC FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 15 models</td></tr>
|GENE= CD3Z, T3Z, TCRZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hac FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hac OCA], [https://pdbe.org/2hac PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hac RCSB], [https://www.ebi.ac.uk/pdbsum/2hac PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hac ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=
== Disease ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hac FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hac OCA], [http://www.ebi.ac.uk/pdbsum/2hac PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hac RCSB]</span>
[https://www.uniprot.org/uniprot/CD3Z_HUMAN CD3Z_HUMAN] Defects in CD247 are the cause of immunodeficiency due to defect in CD3-zeta (CD3ZID) [MIM:[https://omim.org/entry/610163 610163]. An immunological deficiency characterized by T-cells impaired immune response to alloantigens, tetanus toxoid and mitogens.<ref>PMID:16672702</ref>
}}
== Function ==
[https://www.uniprot.org/uniprot/CD3Z_HUMAN CD3Z_HUMAN] Probable role in assembly and expression of the TCR complex as well as signal transduction upon antigen triggering.
== 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/ha/2hac_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=2hac ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The T cell receptor (TCR) alphabeta heterodimer communicates ligand binding to the cell interior via noncovalently associated CD3gammaepsilon, CD3deltaepsilon, and zetazeta dimers. While structures of extracellular components of the TCR-CD3 complex are known, the transmembrane (TM) domains that mediate assembly have eluded structural characterization. Incorporation of the zetazeta signaling module is known to require one basic TCRalpha and two zetazeta aspartic acid TM residues. We report the NMR structure of the zetazeta(TM) dimer, a left-handed coiled coil with substantial polar contacts. Mutagenesis experiments demonstrate that three polar positions are critical for zetazeta dimerization and assembly with TCR. The two aspartic acids create a single structural unit at the zetazeta interface stabilized by extensive hydrogen bonding, and there is evidence for a structural water molecule (or molecules) within close proximity. This structural unit, representing only the second transmembrane dimer interface solved to date, serves as a paradigm for the assembly of all modules involved in TCR signaling.


'''Structure of Zeta-Zeta Transmembrane Dimer'''
The structure of the zetazeta transmembrane dimer reveals features essential for its assembly with the T cell receptor.,Call ME, Schnell JR, Xu C, Lutz RA, Chou JJ, Wucherpfennig KW Cell. 2006 Oct 20;127(2):355-68. PMID:17055436<ref>PMID:17055436</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2hac" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
The T cell receptor (TCR) alphabeta heterodimer communicates ligand binding to the cell interior via noncovalently associated CD3gammaepsilon, CD3deltaepsilon, and zetazeta dimers. While structures of extracellular components of the TCR-CD3 complex are known, the transmembrane (TM) domains that mediate assembly have eluded structural characterization. Incorporation of the zetazeta signaling module is known to require one basic TCRalpha and two zetazeta aspartic acid TM residues. We report the NMR structure of the zetazeta(TM) dimer, a left-handed coiled coil with substantial polar contacts. Mutagenesis experiments demonstrate that three polar positions are critical for zetazeta dimerization and assembly with TCR. The two aspartic acids create a single structural unit at the zetazeta interface stabilized by extensive hydrogen bonding, and there is evidence for a structural water molecule (or molecules) within close proximity. This structural unit, representing only the second transmembrane dimer interface solved to date, serves as a paradigm for the assembly of all modules involved in TCR signaling.
*[[CD3 3D structures|CD3 3D structures]]
 
== References ==
==About this Structure==
<references/>
2HAC is a [[Single protein]] structure of sequence 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=2HAC OCA].
__TOC__
 
</StructureSection>
==Reference==
The structure of the zetazeta transmembrane dimer reveals features essential for its assembly with the T cell receptor., Call ME, Schnell JR, Xu C, Lutz RA, Chou JJ, Wucherpfennig KW, Cell. 2006 Oct 20;127(2):355-68. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17055436 17055436]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Call, M E.]]
[[Category: Call ME]]
[[Category: Chou, J J.]]
[[Category: Chou JJ]]
[[Category: Schnell, J R.]]
[[Category: Schnell JR]]
[[Category: Wucherpfennig, K W.]]
[[Category: Wucherpfennig KW]]
[[Category: alpha helix]]
[[Category: transmembrane]]
 
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Latest revision as of 01:00, 21 November 2024

Structure of Zeta-Zeta Transmembrane Dimer

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