View source for 2na6


==Transmembrane domain of mouse Fas/CD95 death receptor==
<StructureSection load='2na6' size='340' side='right'caption='[[2na6]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2na6]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NA6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NA6 FirstGlance]. <br>
</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=2na6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2na6 OCA], [https://pdbe.org/2na6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2na6 RCSB], [https://www.ebi.ac.uk/pdbsum/2na6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2na6 ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/TNR6_MOUSE TNR6_MOUSE] Note=Defects in Fas are the cause of the lymphoproliferation phenotype (lpr). Lpr mice show lymphadenopathy and autoantibody production.
== Function ==
[https://www.uniprot.org/uniprot/TNR6_MOUSE TNR6_MOUSE] Receptor for TNFSF6/FASLG. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. FAS-mediated apoptosis may have a role in the induction of peripheral tolerance, in the antigen-stimulated suicide of mature T-cells, or both (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Fas (CD95, Apo-1, or TNFRSF6) is a prototypical apoptosis-inducing death receptor in the tumor necrosis factor receptor (TNFR) superfamily. While the extracellular domains of TNFRs form trimeric complexes with their ligands and the intracellular domains engage in higher-order oligomerization, the role of the transmembrane (TM) domains is unknown. We determined the NMR structures of mouse and human Fas TM domains in bicelles that mimic lipid bilayers. Surprisingly, these domains use proline motifs to create optimal packing in homotrimer assembly distinct from classical trimeric coiled-coils in solution. Cancer-associated and structure-based mutations in Fas TM disrupt trimerization in vitro and reduce apoptosis induction in vivo, indicating the essential role of intramembrane trimerization in receptor activity. Our data suggest that the structures represent the signaling-active conformation of Fas TM, which appears to be different from the pre-ligand conformation. Analysis of other TNFR sequences suggests proline-containing sequences as common motifs for receptor TM trimerization.

Structural Basis and Functional Role of Intramembrane Trimerization of the Fas/CD95 Death Receptor.,Fu Q, Fu TM, Cruz AC, Sengupta P, Thomas SK, Wang S, Siegel RM, Wu H, Chou JJ Mol Cell. 2016 Feb 18;61(4):602-13. doi: 10.1016/j.molcel.2016.01.009. Epub 2016 , Feb 4. PMID:26853147<ref>PMID:26853147</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2na6" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Chou JJ]]
[[Category: Fu Q]]
[[Category: Fu T]]
[[Category: Wu H]]