9vfi

Structure of hTRPC3 solubilized with 4F peptide at 2.72 angstrom

spinqualitylabelsall models 9vfi, resolution 2.72Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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