ArticleProceedings of the National Academy of Sciences of the United States of America2018
QTY code enables design of detergent-free chemokine receptors that retain ligand-binding activities.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 86 citations in OpenAlex.
- In silico directed evolution of humanized peptide transporters via computational epistatic rescue.Molecular diversity · 2026Article
- Dynamics-aware evolutionary profiling uncouples structural rigidity from functional motion to enable enhanced variant interpretation.Functional & integrative genomics · 2026Article
- Identification of Entacapone as a Novel β-Arrestin 1 Biased Antagonist of CXCR7.Molecules (Basel, Switzerland) · 2026Article
- Integrative Structural Bioinformatics and Molecular Dynamics Analyses of Synaptic Vesicle Proteins and Their Water-Soluble QTY-Variants Reveal Membrane Constraints and Evolutionary Coupling of T ⇔ V.Journal of molecular evolution · 2026Article
- Microenvironmental pH and host-pathogen co-evolution potentially influence the structural architecture of junctional adhesion molecules.Molecular genetics and genomics : MGG · 2026Article
- Activation dynamics of a water-soluble human mu-opioid receptor.The Journal of biological chemistry · 2026Article
- Lipochaperoning folding of water-soluble functional membrane protein in genetically and biosynthetically tuned EscherichiaiScience · 2026Article
- Beyond Small Molecules: Orchestrating Cell Fate with Engineered Water-Soluble Membrane Proteins.Biomolecules · 2026Article
- Article
- Co-evolution of alpha-helical transmembrane protein residues: large-scale variant profiling and complete mutational landscape of 2277 known PDB entries representing 504 unique human protein sequences.Journal of molecular evolution · 2025Article
- Design of a water-soluble CD20 antigen with computational epitope scaffolding.Protein science : a publication of the Protein Society · 2025Article
- Engineering of soluble bacteriorhodopsin.Chemical science · 2025Article
- Solubilization of Membrane Proteins using designed protein WRAPS.bioRxiv : the preprint server for biology · 2025Article
- Structure Bioinformatics of Six Human Integral Transmembrane Enzymes and their AlphaFold3 Predicted Water-Soluble QTY Analogs: Insights into FACE1 and STEA4 Binding Mechanisms.Pharmaceutical research · 2025Article
- Structural bioinformatic study of human mitochondrial respiratory integral membrane megacomplex and its AlphaFold3 predicted water-soluble QTY megacomplex analog.QRB discovery · 2025Article
- A structural and functional bioinformatics study of QTY-designed retinylidene proteins.QRB discovery · 2025Article
- Article
- Computational engineering of water-soluble human potassium ion channels through QTY transformation.Scientific reports · 2024Article
- Molecular Dynamic Simulations Reveal that Water-Soluble QTY-Variants of Glutamate Transporters EAA1, EAA2 and EAA3 Retain the Conformational Characteristics of Native Transporters.Pharmaceutical research · 2024Article
- Dynamics design of a non-natural transcription factor responding to androst-4-ene-3,17-dione.Synthetic and systems biotechnology · 2024Article
Corrections and comments
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Authors and funding
17 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Structure and function studies of membrane proteins, particularly G protein-coupled receptors and multipass transmembrane proteins, require detergents. We have devised a simple tool, the QTY code (glutamine, threonine, and tyrosine), for designing hydrophobic domains to become water soluble without detergents. Here we report using the QTY code to systematically replace the hydrophobic amino acids leucine, valine, isoleucine, and phenylalanine in the seven transmembrane α-helices of CCR5, CXCR4, CCR10, and CXCR7. We show that QTY code-designed chemokine receptor variants retain their thermostabilities, α-helical structures, and ligand-binding activities in buffer and 50% human serum. CCR5
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.