9VFI

Structure of hTRPC3 solubilized with 4F peptide at 2.72 angstrom

This is a non-PDB format compatible entry.

Summary for 9VFI

• Entry DOI: 10.2210/pdb9vfi/pdb
• EMDB information: 65025
• Descriptor: Green fluorescence protein,Maltose/maltodextrin-binding periplasmic protein,Short transient receptor potential channel 3,Maltose/maltodextrin-binding periplasmic protein,Short transient receptor potential channel 3,Maltose/maltodextrin-binding periplasmic protein,Short transient receptor potential channel 3, CALCIUM ION, ZINC ION, ... (5 entities in total)
• Functional Keywords: trpc3, 4f peptide, native lipid environment, metal transport
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 4
• Total formula weight: 696507.20

Authors

Chen, L.,Zang, J. (deposition date: 2025-06-11, release date: 2026-04-22)

Primary citation

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., 437:169467-169467, 2025

PubMed Abstract: 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.

PubMed: 41061950
DOI: 10.1016/j.jmb.2025.169467

Experimental method

ELECTRON MICROSCOPY (2.72 Å)