9or5: Difference between revisions

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'''Unreleased structure'''


The entry 9or5 is ON HOLD  until Paper Publication
==Cryo-EM structure of rat TRPM1 in the apo state==
<StructureSection load='9or5' size='340' side='right'caption='[[9or5]], [[Resolution|resolution]] 4.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9or5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9OR5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9OR5 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]] 4.3&#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=9or5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9or5 OCA], [https://pdbe.org/9or5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9or5 RCSB], [https://www.ebi.ac.uk/pdbsum/9or5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9or5 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Transient receptor potential melastatin 1 (TRPM1) is a membrane protein essential for vision in dim light, and mutations in TRPM1 cause complete congenital stationary night blindness. Although TRPM1 shares sequence similarity to other TRPM ion channels such as TRPM3, whether it independently functions as an ion channel remains controversial. This controversy is largely caused by TRPM1's challenging biochemical behaviors that prevent detailed molecular characterization. In this work, we isolate TRPM1 and determine its structures using cryogenic electron microscopy (cryo-EM). The structures reveal a canonical tetrameric fold in the intracellular domain, consistent with other TRPM family members that are ion channels. Surprisingly, in the transmembrane domain, despite the presence of the conserved voltage sensor-like domain (VSLD) and pore domain (PD) in a domain-swapped fashion, the VSLD and PD are arranged with an opposite handedness compared to other related channels. This inverted transmembrane domain allows the formation of a large pore-like structure that supports the role of TRPM1 as an ion channel. This non-canonical architecture of TRPM1 may also confer unique permeation and pharmacological properties.


Authors:  
Cryo-EM structure of TRPM1 reveals a non-canonical architecture with an inverted transmembrane domain.,Fabrizio M, Brewer M, Bogdanovic N, Zhao C Nat Commun. 2026 Mar 19. doi: 10.1038/s41467-026-70722-7. PMID:41857038<ref>PMID:41857038</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 9or5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Fabrizio M]]
[[Category: Zhao C]]
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