ArticleJournal of chemical information and modeling2019
Prediction of Conformation Specific Thermostabilizing Mutations for Class A G Protein-Coupled Receptors.
Article in Journal of chemical information and modeling, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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Who cites it
3 citing papers in PubMed.
- Sequence coevolution and structure stabilization modulate olfactory receptor expression.Biophysical journal · 2022Article
- VARIDT 2.0: structural variability of drug transporter.Nucleic acids research · 2022Article
- Multi-omics approach to identifying isoform variants as therapeutic targets in cancer patients.Frontiers in oncology · 2022Review
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Authors and funding
5 authors.
Funding
Abstract
G protein-coupled receptors (GPCRs) are highly flexible and prone to denaturation during protein extraction in detergents and purification. This poses a huge challenge to purify a conformationally homogeneous solution of GPCRs. Thermostabilizing mutations have been used widely to purify and obtain crystal structures of several GPCRs. However, identifying thermostabilizing mutations for GPCRs remains a tedious and expensive task as they are not transferable even among closely related GPCRs. Additionally, the mutations stabilizing one conformational state of a GPCR do not always stabilize other conformational state(s) of the same GPCR. Previously we developed a computational method, LiticonDesign, for rapid prediction of thermostabilizing mutations for a specific GPCR conformation. In this study, we have used LiticonDesign to predict thermostabilizing mutations for the agonist bound active-intermediate state of the human adenosine receptor (A
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