View source for 2n97


==DD homodimer==
<StructureSection load='2n97' size='340' side='right'caption='[[2n97]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2n97]] 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=2N97 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N97 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=2n97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n97 OCA], [https://pdbe.org/2n97 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n97 RCSB], [https://www.ebi.ac.uk/pdbsum/2n97 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n97 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TNR16_HUMAN TNR16_HUMAN] Plays a role in the regulation of the translocation of GLUT4 to the cell surface in adipocytes and skeletal muscle cells in response to insulin, probably by regulating RAB31 activity, and thereby contributes to the regulation of insulin-dependent glucose uptake (By similarity). Low affinity receptor which can bind to NGF, BDNF, NT-3, and NT-4. Can mediate cell survival as well as cell death of neural cells.<ref>PMID:14966521</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Death domains (DDs) mediate assembly of oligomeric complexes for activation of downstream signaling pathways through incompletely understood mechanisms. Here we report structures of complexes formed by the DD of p75 neurotrophin receptor (p75NTR) with RhoGDI, for activation of the RhoA pathway, with caspase recruitment domain (CARD) of RIP2 kinase, for activation of the NF-kB pathway, and with itself, revealing how DD dimerization controls access of intracellular effectors to the receptor. RIP2 CARD and RhoGDI bind to p75NTR DD at partially overlapping epitopes with over 100-fold difference in affinity, revealing the mechanism by which RIP2 recruitment displaces RhoGDI upon ligand binding. The p75NTR DD forms non-covalent, low-affinity symmetric dimers in solution. The dimer interface overlaps with RIP2 CARD but not RhoGDI binding sites, supporting a model of receptor activation triggered by separation of DDs. These structures reveal how competitive protein-protein interactions orchestrate the hierarchical activation of downstream pathways in non-catalytic receptors.

Structural basis of death domain signaling in the p75 neurotrophin receptor.,Lin Z, Tann JY, Goh ET, Kelly C, Lim KB, Gao JF, Ibanez CF Elife. 2015 Dec 8;4. pii: e11692. doi: 10.7554/eLife.11692. PMID:26646181<ref>PMID:26646181</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2n97" style="background-color:#fffaf0;"></div>

==See Also==
*[[Tumor necrosis factor receptor 3D structures|Tumor necrosis factor receptor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Ibanez CF]]
[[Category: Lin Z]]