11ib: Difference between revisions

Latest revision as of 16:37, 8 September 2026

2-APB bound human TRPV2, S651H/T654D/D655N

Structural highlights

11ib is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.33Å
Ligands:	CLR, FZ4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TRPV2_HUMAN Calcium-permeable, non-selective cation channel with an outward rectification. Seems to be regulated, at least in part, by IGF-I, PDGF and neuropeptide head activator. May transduce physical stimuli in mast cells. Activated by temperatures higher than 52 degrees Celsius; is not activated by vanilloids and acidic pH.^[1]

Publication Abstract from PubMed

Transient receptor potential vanilloid 2 (TRPV2) is a broadly expressed ion channel implicated in diverse physiological and pathological processes. Despite strong conservation, human TRPV2 (hTRPV2) displays markedly reduced sensitivity to stimuli such as 2-aminoethoxydiphenyl borate (2-APB) and heat compared to rodent orthologs. Here we combine electrophysiology and cryo electron microscopy to define the basis of this species-dependent divergence. The structure of hTRPV2 is remarkably different at the voltage sensor-like domain (VSLD) compared to rodent channels and functional analyses show a graded activity profile between human, mouse and rat TRPV2 to a broad range of chemical and physical stimuli. Three residues located between S6 and the TRP domain tune this functional difference, as reciprocal substitutions exchange current phenotypes. hTRPV2 structures of this mutant reveal coupling between the mutation site and the VSLD as well as an additional binding site for 2-APB. Together, these findings define structural determinants of species-specific TRPV2 function.

Structural origins of species-specific differences in TRPV2 activation.,Fricke TC, Pumroy RA, Rocereta JA, De Jesus-Perez JJ, Oprita G, Meyer MJA, Herzog C, Echtermeyer FG, Hill K, Leffler A, Moiseenkova-Bell VY Nat Commun. 2026 Aug 20;17(1):8737. doi: 10.1038/s41467-026-76831-7. PMID:42624855^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Caterina MJ, Rosen TA, Tominaga M, Brake AJ, Julius D. A capsaicin-receptor homologue with a high threshold for noxious heat. Nature. 1999 Apr 1;398(6726):436-41. PMID:10201375 doi:https://dx.doi.org/10.1038/18906
↑ Fricke TC, Pumroy RA, Rocereta JA, De Jesus-Perez JJ, Oprita G, Meyer MJA, Herzog C, Echtermeyer FG, Hill K, Leffler A, Moiseenkova-Bell VY. Structural origins of species-specific differences in TRPV2 activation. Nat Commun. 2026 Aug 20;17(1):8737. doi: 10.1038/s41467-026-76831-7. PMID:42624855 doi:https://dx.doi.org/10.1038/s41467-026-76831-7

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Caterina MJ, Rosen TA, Tominaga M, Brake AJ, Julius D. A capsaicin-receptor homologue with a high threshold for noxious heat. Nature. 1999 Apr 1;398(6726):436-41. PMID:10201375 doi:https://dx.doi.org/10.1038/18906

[2] Fricke TC, Pumroy RA, Rocereta JA, De Jesus-Perez JJ, Oprita G, Meyer MJA, Herzog C, Echtermeyer FG, Hill K, Leffler A, Moiseenkova-Bell VY. Structural origins of species-specific differences in TRPV2 activation. Nat Commun. 2026 Aug 20;17(1):8737. doi: 10.1038/s41467-026-76831-7. PMID:42624855 doi:https://dx.doi.org/10.1038/s41467-026-76831-7

[1]

[2]

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 11ib is ON HOLD  until Paper Publication
+==2-APB bound human TRPV2, S651H/T654D/D655N==
+<StructureSection load='11ib' size='340' side='right'caption='[[11ib]], [[Resolution|resolution]] 3.33&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[11ib]] 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=11IB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=11IB 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]] 3.33&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=FZ4:2-diphenylboranyloxyethanamine'>FZ4</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=11ib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=11ib OCA], [https://pdbe.org/11ib PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=11ib RCSB], [https://www.ebi.ac.uk/pdbsum/11ib PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=11ib ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TRPV2_HUMAN TRPV2_HUMAN] Calcium-permeable, non-selective cation channel with an outward rectification. Seems to be regulated, at least in part, by IGF-I, PDGF and neuropeptide head activator. May transduce physical stimuli in mast cells. Activated by temperatures higher than 52 degrees Celsius; is not activated by vanilloids and acidic pH.<ref>PMID:10201375</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Transient receptor potential vanilloid 2 (TRPV2) is a broadly expressed ion channel implicated in diverse physiological and pathological processes. Despite strong conservation, human TRPV2 (hTRPV2) displays markedly reduced sensitivity to stimuli such as 2-aminoethoxydiphenyl borate (2-APB) and heat compared to rodent orthologs. Here we combine electrophysiology and cryo electron microscopy to define the basis of this species-dependent divergence. The structure of hTRPV2 is remarkably different at the voltage sensor-like domain (VSLD) compared to rodent channels and functional analyses show a graded activity profile between human, mouse and rat TRPV2 to a broad range of chemical and physical stimuli. Three residues located between S6 and the TRP domain tune this functional difference, as reciprocal substitutions exchange current phenotypes. hTRPV2 structures of this mutant reveal coupling between the mutation site and the VSLD as well as an additional binding site for 2-APB. Together, these findings define structural determinants of species-specific TRPV2 function.
-Authors:
+Structural origins of species-specific differences in TRPV2 activation.,Fricke TC, Pumroy RA, Rocereta JA, De Jesus-Perez JJ, Oprita G, Meyer MJA, Herzog C, Echtermeyer FG, Hill K, Leffler A, Moiseenkova-Bell VY Nat Commun. 2026 Aug 20;17(1):8737. doi: 10.1038/s41467-026-76831-7. PMID:42624855<ref>PMID:42624855</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 11ib" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Moiseenkova-Bell VY]]
+[[Category: Pumroy RP]]
+[[Category: Rocereta JA]]

11ib: Difference between revisions

Latest revision as of 16:37, 8 September 2026

2-APB bound human TRPV2, S651H/T654D/D655N

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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