9vfi: Difference between revisions

Latest revision as of 06:41, 22 April 2026

Structure of hTRPC3 solubilized with 4F peptide at 2.72 angstrom

Structural highlights

9vfi 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 2.72Å
Ligands:	A1L5I, CA, ZN
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

TRPC3_HUMAN The disease is caused by mutations affecting the gene represented in this entry.

Function

TRPC3_HUMAN Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Activated by diacylglycerol (DAG) in a membrane-delimited fashion, independently of protein kinase C, and by inositol 1,4,5-triphosphate receptors (ITPR) with bound IP3. May also be activated by internal calcium store depletion.^[1] ^[2] ^[3] ^[4] MALE_ECO57 Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides (By similarity).

Publication Abstract from PubMed

Integral membrane proteins are vital for numerous biological functions and their structures are typically studied using X-ray crystallography and cryo-electron microscopy (cryo-EM). However, these techniques require the extraction of target membrane proteins from their native membranes using detergents, which might disrupt the lipid environments and alter protein behavior. In this study, we present a novel method for solubilizing membrane proteins using 4F peptide, thereby eliminating the need for detergents throughout the procedure. We demonstrate that the 4F peptide effectively solubilizes a range of membrane proteins and complexes into 4F-discs, while preserving their functionality and structural integrity. Converting these 4F-discs into nanodiscs further enhances particle homogeneity and facilitates high-resolution structural determination of membrane proteins. Our findings highlight the potential of membrane-solubilizing peptides to advance membrane protein research.

Unveiling Eukaryotic Membrane Proteins in High Resolution Using Peptide Solubilization.,Zang J, Shi Y, Tao W, Liu X, Guo W, Chen L J Mol Biol. 2025 Dec 15;437(24):169467. doi: 10.1016/j.jmb.2025.169467. Epub 2025 , Oct 6. PMID:41061950^[5]

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

References

↑ Woo JS, Hwang JH, Ko JK, Weisleder N, Kim DH, Ma J, Lee EH. S165F mutation of junctophilin 2 affects Ca2+ signalling in skeletal muscle. Biochem J. 2010 Mar 15;427(1):125-34. doi: 10.1042/BJ20091225. PMID:20095964 doi:https://dx.doi.org/10.1042/BJ20091225
↑ Zhu X, Jiang M, Peyton M, Boulay G, Hurst R, Stefani E, Birnbaumer L. trp, a novel mammalian gene family essential for agonist-activated capacitative Ca2+ entry. Cell. 1996 May 31;85(5):661-71. PMID:8646775
↑ Zhu X, Jiang M, Birnbaumer L. Receptor-activated Ca2+ influx via human Trp3 stably expressed in human embryonic kidney (HEK)293 cells. Evidence for a non-capacitative Ca2+ entry. J Biol Chem. 1998 Jan 2;273(1):133-42. PMID:9417057
↑ Hofmann T, Obukhov AG, Schaefer M, Harteneck C, Gudermann T, Schultz G. Direct activation of human TRPC6 and TRPC3 channels by diacylglycerol. Nature. 1999 Jan 21;397(6716):259-63. doi: 10.1038/16711. PMID:9930701 doi:https://dx.doi.org/10.1038/16711
↑ Zang J, Shi Y, Tao W, Liu X, Guo W, Chen L. Unveiling Eukaryotic Membrane Proteins in High Resolution Using Peptide Solubilization. J Mol Biol. 2025 Dec 15;437(24):169467. PMID:41061950 doi:10.1016/j.jmb.2025.169467

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Woo JS, Hwang JH, Ko JK, Weisleder N, Kim DH, Ma J, Lee EH. S165F mutation of junctophilin 2 affects Ca2+ signalling in skeletal muscle. Biochem J. 2010 Mar 15;427(1):125-34. doi: 10.1042/BJ20091225. PMID:20095964 doi:https://dx.doi.org/10.1042/BJ20091225

[2] Zhu X, Jiang M, Peyton M, Boulay G, Hurst R, Stefani E, Birnbaumer L. trp, a novel mammalian gene family essential for agonist-activated capacitative Ca2+ entry. Cell. 1996 May 31;85(5):661-71. PMID:8646775

[3] Zhu X, Jiang M, Birnbaumer L. Receptor-activated Ca2+ influx via human Trp3 stably expressed in human embryonic kidney (HEK)293 cells. Evidence for a non-capacitative Ca2+ entry. J Biol Chem. 1998 Jan 2;273(1):133-42. PMID:9417057

[4] Hofmann T, Obukhov AG, Schaefer M, Harteneck C, Gudermann T, Schultz G. Direct activation of human TRPC6 and TRPC3 channels by diacylglycerol. Nature. 1999 Jan 21;397(6716):259-63. doi: 10.1038/16711. PMID:9930701 doi:https://dx.doi.org/10.1038/16711

[5] Zang J, Shi Y, Tao W, Liu X, Guo W, Chen L. Unveiling Eukaryotic Membrane Proteins in High Resolution Using Peptide Solubilization. J Mol Biol. 2025 Dec 15;437(24):169467. PMID:41061950 doi:10.1016/j.jmb.2025.169467

[1]

[2]

[3]

[4]

[5]

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 9vfi is ON HOLD  until Paper Publication
+==Structure of hTRPC3 solubilized with 4F peptide at 2.72 angstrom==
+<StructureSection load='9vfi' size='340' side='right'caption='[[9vfi]], [[Resolution|resolution]] 2.72&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[9vfi]] 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=9VFI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9VFI 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]] 2.72&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1L5I:[(2~{S})-2-[(~{E})-octadec-9-enoyl]oxy-3-oxidanyl-propyl]+octadec-9-enoate'>A1L5I</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=9vfi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9vfi OCA], [https://pdbe.org/9vfi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9vfi RCSB], [https://www.ebi.ac.uk/pdbsum/9vfi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9vfi ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/TRPC3_HUMAN TRPC3_HUMAN] The disease is caused by mutations affecting the gene represented in this entry.
+== Function ==
+[https://www.uniprot.org/uniprot/TRPC3_HUMAN TRPC3_HUMAN] Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Activated by diacylglycerol (DAG) in a membrane-delimited fashion, independently of protein kinase C, and by inositol 1,4,5-triphosphate receptors (ITPR) with bound IP3. May also be activated by internal calcium store depletion.<ref>PMID:20095964</ref> <ref>PMID:8646775</ref> <ref>PMID:9417057</ref> <ref>PMID:9930701</ref> [https://www.uniprot.org/uniprot/MALE_ECO57 MALE_ECO57] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides (By similarity).
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Integral membrane proteins are vital for numerous biological functions and their structures are typically studied using X-ray crystallography and cryo-electron microscopy (cryo-EM). However, these techniques require the extraction of target membrane proteins from their native membranes using detergents, which might disrupt the lipid environments and alter protein behavior. In this study, we present a novel method for solubilizing membrane proteins using 4F peptide, thereby eliminating the need for detergents throughout the procedure. We demonstrate that the 4F peptide effectively solubilizes a range of membrane proteins and complexes into 4F-discs, while preserving their functionality and structural integrity. Converting these 4F-discs into nanodiscs further enhances particle homogeneity and facilitates high-resolution structural determination of membrane proteins. Our findings highlight the potential of membrane-solubilizing peptides to advance membrane protein research.
-Authors:
+Unveiling Eukaryotic Membrane Proteins in High Resolution Using Peptide Solubilization.,Zang J, Shi Y, Tao W, Liu X, Guo W, Chen L J Mol Biol. 2025 Dec 15;437(24):169467. doi: 10.1016/j.jmb.2025.169467. Epub 2025 , Oct 6. PMID:41061950<ref>PMID:41061950</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 9vfi" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Chen L]]
+[[Category: Zang J]]

9vfi: Difference between revisions

Latest revision as of 06:41, 22 April 2026

Structure of hTRPC3 solubilized with 4F peptide at 2.72 angstrom

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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