View source for 8cni


==PHT1 in the outward facing conformation, bound to Sb27==
<StructureSection load='8cni' size='340' side='right'caption='[[8cni]], [[Resolution|resolution]] 3.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8cni]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8CNI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CNI FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.35&#8491;</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=8cni FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8cni OCA], [https://pdbe.org/8cni PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8cni RCSB], [https://www.ebi.ac.uk/pdbsum/8cni PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8cni ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A8V0ZFZ8_CHICK A0A8V0ZFZ8_CHICK] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
PHT1 is a histidine /oligopeptide transporter with an essential role in Toll-like receptor innate immune responses. It can act as a receptor by recruiting the adaptor protein TASL which leads to type I interferon production via IRF5. Persistent stimulation of this signalling pathway is known to be involved in the pathogenesis of systemic lupus erythematosus (SLE). Understanding how PHT1 recruits TASL at the molecular level, is therefore clinically important for the development of therapeutics against SLE and other autoimmune diseases. Here we present the Cryo-EM structure of PHT1 stabilized in the outward-open conformation. By combining biochemical and structural modeling techniques we propose a model of the PHT1-TASL complex, in which the first 16 N-terminal TASL residues fold into a helical structure that bind in the central cavity of the inward-open conformation of PHT1. This work provides critical insights into the molecular basis of PHT1/TASL mediated type I interferon production.

Molecular basis of TASL recruitment by the peptide/histidine transporter 1, PHT1.,Custodio TF, Killer M, Yu D, Puente V, Teufel DP, Pautsch A, Schnapp G, Grundl M, Kosinski J, Low C Nat Commun. 2023 Sep 14;14(1):5696. doi: 10.1038/s41467-023-41420-5. PMID:37709742<ref>PMID:37709742</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8cni" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Custodio T]]
[[Category: Killer M]]
[[Category: Loew C]]