View source for 7vq2


==Structure of Apo-hsTRPM2 channel TM domain==
<StructureSection load='7vq2' size='340' side='right'caption='[[7vq2]], [[Resolution|resolution]] 3.68&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VQ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VQ2 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]] 3.68&#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=7vq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vq2 OCA], [https://pdbe.org/7vq2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vq2 RCSB], [https://www.ebi.ac.uk/pdbsum/7vq2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vq2 ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Transient receptor potential melastatin 2 (TRPM2), a Ca(2+)-permeable cation channel, is gated by intracellular adenosine diphosphate ribose (ADPR), Ca(2+), warm temperature, and oxidative stress. It is critically involved in physiological and pathological processes ranging from inflammation to stroke to neurodegeneration. At present, the channel's gating and ion permeation mechanisms, such as the location and identity of the selectivity filter, remain ambiguous. Here, we report the cryo-electron microscopy (cryo-EM) structure of human TRPM2 in nanodisc in the ligand-free state. Cryo-EM map-guided computational modeling and patch-clamp recording further identify a quadruple-residue motif as the ion selectivity filter, which adopts a restrictive conformation in the closed state and acts as a gate, profoundly contrasting with its widely open conformation in the Nematostella vectensis TRPM2. Our study reveals the gating of human TRPM2 by the filter and demonstrates the feasibility of using cryo-EM in conjunction with computational modeling and functional studies to garner structural information for intrinsically dynamic but functionally important domains.

Structural and functional basis of the selectivity filter as a gate in human TRPM2 channel.,Yu X, Xie Y, Zhang X, Ma C, Liu L, Zhen W, Xu L, Zhang J, Liang Y, Zhao L, Gao X, Yu P, Luo J, Jiang LH, Nie Y, Yang F, Guo J, Yang W Cell Rep. 2021 Nov 16;37(7):110025. doi: 10.1016/j.celrep.2021.110025. PMID:34788616<ref>PMID:34788616</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7vq2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Guo JT]]
[[Category: Ma C]]
[[Category: Xie Y]]
[[Category: Yang F]]
[[Category: Yang W]]
[[Category: Yu XF]]
[[Category: Zhang XK]]