7v6y: Difference between revisions
New page: '''Unreleased structure''' The entry 7v6y is ON HOLD Authors: Luo, Y., Zhao, Y., Qu, Q., Li, D. Description: Cryo-EM structure of Patched in lipid nanodisc -the wildtype, 3.5 angstrom ... |
No edit summary |
||
| (2 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Cryo-EM structure of Patched in lipid nanodisc - the wildtype, 3.5 angstrom (re-processed with dataset of 7dzq)== | |||
<StructureSection load='7v6y' size='340' side='right'caption='[[7v6y]], [[Resolution|resolution]] 3.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7v6y]] is a 1 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=7dzq 7dzq]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7V6Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7V6Y FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5VI:(2S)-2-azanyl-3-[[(2S)-3-butanoyloxy-2-dec-9-enoyloxy-propoxy]-oxidanyl-phosphoryl]oxy-propanoic+acid'>5VI</scene>, <scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7dzq|7dzq]]</div></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=7v6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v6y OCA], [https://pdbe.org/7v6y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v6y RCSB], [https://www.ebi.ac.uk/pdbsum/7v6y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v6y ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[https://www.uniprot.org/uniprot/PTC1_MOUSE PTC1_MOUSE]] Acts as a receptor for sonic hedgehog (SHH), indian hedgehog (IHH) and desert hedgehog (DHH). Associates with the smoothened protein (SMO) to transduce the hedgehog's proteins signal. Seems to have a tumor suppressor function, as inactivation of this protein is probably a necessary, if not sufficient step for tumorigenesis.<ref>PMID:21537345</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The 12-transmembrane protein Patched (Ptc1) acts as a suppressor for Hedgehog (Hh) signaling by depleting sterols in the cytoplasmic membrane leaflet that are required for the activation of downstream regulators. The positive modulator Hh inhibits Ptc1's transporter function by binding to Ptc1 and its co-receptors, which are locally concentrated in invaginated microdomains known as caveolae. Here, we reconstitute the mouse Ptc1 into lipid nanodiscs and determine its structure using single-particle cryoelectron microscopy. The structure is overall similar to those in amphipol and detergents but displays various conformational differences in the transmembrane region. Although most particles show monomers, we observe Ptc1 dimers with distinct interaction patterns and different membrane curvatures, some of which are reminiscent of caveolae. We find that an extramembranous "hand-shake" region rich in hydrophobic and aromatic residues mediates inter-Ptc1 interactions under different membrane curvatures. Our data provide a plausible framework for Ptc1 clustering in the highly curved caveolae. | |||
Cryo-EM study of patched in lipid nanodisc suggests a structural basis for its clustering in caveolae.,Luo Y, Wan G, Zhang X, Zhou X, Wang Q, Fan J, Cai H, Ma L, Wu H, Qu Q, Cong Y, Zhao Y, Li D Structure. 2021 Jun 22. pii: S0969-2126(21)00208-2. doi:, 10.1016/j.str.2021.06.004. PMID:34174188<ref>PMID:34174188</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7v6y" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Protein patched homolog 1|Protein patched homolog 1]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Li, D]] | [[Category: Li, D]] | ||
[[Category: Luo, Y]] | [[Category: Luo, Y]] | ||
[[Category: Qu, Q]] | |||
[[Category: Zhao, Y]] | [[Category: Zhao, Y]] | ||
[[Category: | [[Category: Caveolae]] | ||
[[Category: Hedgehog signaling]] | |||
[[Category: Lipid nanodisc]] | |||
[[Category: Membrane protein]] | |||
[[Category: Patched]] | |||
[[Category: Ptc1 dimer]] | |||
Latest revision as of 14:12, 16 February 2022
Cryo-EM structure of Patched in lipid nanodisc - the wildtype, 3.5 angstrom (re-processed with dataset of 7dzq)Cryo-EM structure of Patched in lipid nanodisc - the wildtype, 3.5 angstrom (re-processed with dataset of 7dzq)
Structural highlights
Function[PTC1_MOUSE] Acts as a receptor for sonic hedgehog (SHH), indian hedgehog (IHH) and desert hedgehog (DHH). Associates with the smoothened protein (SMO) to transduce the hedgehog's proteins signal. Seems to have a tumor suppressor function, as inactivation of this protein is probably a necessary, if not sufficient step for tumorigenesis.[1] Publication Abstract from PubMedThe 12-transmembrane protein Patched (Ptc1) acts as a suppressor for Hedgehog (Hh) signaling by depleting sterols in the cytoplasmic membrane leaflet that are required for the activation of downstream regulators. The positive modulator Hh inhibits Ptc1's transporter function by binding to Ptc1 and its co-receptors, which are locally concentrated in invaginated microdomains known as caveolae. Here, we reconstitute the mouse Ptc1 into lipid nanodiscs and determine its structure using single-particle cryoelectron microscopy. The structure is overall similar to those in amphipol and detergents but displays various conformational differences in the transmembrane region. Although most particles show monomers, we observe Ptc1 dimers with distinct interaction patterns and different membrane curvatures, some of which are reminiscent of caveolae. We find that an extramembranous "hand-shake" region rich in hydrophobic and aromatic residues mediates inter-Ptc1 interactions under different membrane curvatures. Our data provide a plausible framework for Ptc1 clustering in the highly curved caveolae. Cryo-EM study of patched in lipid nanodisc suggests a structural basis for its clustering in caveolae.,Luo Y, Wan G, Zhang X, Zhou X, Wang Q, Fan J, Cai H, Ma L, Wu H, Qu Q, Cong Y, Zhao Y, Li D Structure. 2021 Jun 22. pii: S0969-2126(21)00208-2. doi:, 10.1016/j.str.2021.06.004. PMID:34174188[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||