View source for 2l34


==Structure of the DAP12 transmembrane homodimer==
<StructureSection load='2l34' size='340' side='right'caption='[[2l34]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2l34]] 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=2L34 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L34 FirstGlance]. <br>
</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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2l34 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l34 OCA], [https://pdbe.org/2l34 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l34 RCSB], [https://www.ebi.ac.uk/pdbsum/2l34 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l34 ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/TYOBP_HUMAN TYOBP_HUMAN] Nasu-Hakola disease. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
[https://www.uniprot.org/uniprot/TYOBP_HUMAN TYOBP_HUMAN] Non-covalently associates with activating receptors of the CD300 family. Cross-linking of CD300-TYROBP complexes results in cellular activation. Involved for instance in neutrophil activation mediated by integrin.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Many receptors that activate cells of the immune system are multisubunit membrane protein complexes in which ligand recognition and signaling functions are contributed by separate protein modules. Receptors and signaling subunits assemble through contacts among basic and acidic residues in their transmembrane domains to form the functional complexes. Here we report the nuclear magnetic resonance (NMR) structure of the membrane-embedded, heterotrimeric assembly formed by association of the DAP12 signaling module with the natural killer (NK) cell-activating receptor NKG2C. The main intramembrane contact site is formed by a complex electrostatic network involving five hydrophilic transmembrane residues. Functional mutagenesis demonstrated that similar polar intramembrane motifs are also important for assembly of the NK cell-activating NKG2D-DAP10 complex and the T cell antigen receptor (TCR)-invariant signaling protein CD3 complex. This structural motif therefore lies at the core of the molecular organization of many activating immunoreceptors.

The structural basis for intramembrane assembly of an activating immunoreceptor complex.,Call ME, Wucherpfennig KW, Chou JJ Nat Immunol. 2010 Nov;11(11):1023-9. Epub 2010 Oct 3. PMID:20890284<ref>PMID:20890284</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2l34" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Call ME]]
[[Category: Chou JJ]]
[[Category: Wucherpfennig KW]]