6up7: Difference between revisions
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==neurotensin receptor and arrestin2 complex== | |||
<SX load='6up7' size='340' side='right' viewer='molstar' caption='[[6up7]], [[Resolution|resolution]] 4.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6up7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UP7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UP7 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]] 4.2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PIO:[(2R)-2-OCTANOYLOXY-3-[OXIDANYL-[(1R,2R,3S,4R,5R,6S)-2,3,6-TRIS(OXIDANYL)-4,5-DIPHOSPHONOOXY-CYCLOHEXYL]OXY-PHOSPHORYL]OXY-PROPYL]+OCTANOATE'>PIO</scene></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=6up7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6up7 OCA], [https://pdbe.org/6up7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6up7 RCSB], [https://www.ebi.ac.uk/pdbsum/6up7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6up7 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/NEUT_HUMAN NEUT_HUMAN] Neurotensin may play an endocrine or paracrine role in the regulation of fat metabolism. It causes contraction of smooth muscle. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Arrestin proteins bind to active, phosphorylated G-protein-coupled receptors (GPCRs), thereby preventing G-protein coupling, triggering receptor internalization, and affecting various downstream signalling pathways(1,2). Although there is a wealth of structural information delineating the interactions between GPCRs and G proteins, less is known about how arrestins engage GPCRs. Here we report a cryo-EM structure of full-length human neurotensin receptor 1 (NTSR1) in complex with truncated human beta-arrestin 1 (betaarr1(DeltaCT)). We found that phosphorylation of NTSR1 was critical for obtaining a stable complex with betaarr1(DeltaCT), and identified phosphorylated sites in both the third intracellular loop and the C terminus that may promote this interaction. In addition, we observed a phosphatidylinositol-4,5-bisphosphate (PI(4,5)P2) molecule forming a bridge between the membrane side of NTSR1 transmembrane segments 1 and 4 and the C-lobe of arrestin. Compared to a structure of rhodopsin-arrestin-1, our structure displays an approximately 85 degrees rotation of arrestin relative to the receptor. These findings highlight both conserved aspects but also the plasticity of arrestin-receptor interactions. | |||
Structure of the neurotensin receptor 1 in complex with beta-arrestin 1.,Huang W, Masureel M, Qianhui Q, Janetzko J, Inoue A, Kato HE, Robertson MJ, Nguyen KC, Glenn JS, Skiniotis G, Kobilka BK Nature. 2020 Jan 16. pii: 10.1038/s41586-020-1953-1. doi:, 10.1038/s41586-020-1953-1. PMID:31945771<ref>PMID:31945771</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Qu | <div class="pdbe-citations 6up7" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Arrestin 3D structures|Arrestin 3D structures]] | |||
*[[Neurotensin receptor|Neurotensin receptor]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</SX> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Huang W]] | |||
[[Category: Janetzko J]] | |||
[[Category: Kobilka BK]] | |||
[[Category: Masureel M]] | |||
[[Category: Qu QH]] | |||
[[Category: Skiniotis G]] | |||