ArticleBiophysical journal2019
Interfacial Binding Sites for Cholesterol on TRP Ion Channels.
Article in Biophysical journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- Role of cholesterol-recognition motifs in the infectivity of SARS-CoV-2 variants.Colloids and surfaces. B, Biointerfaces · 2023Article
- Regulation of ThermoTRP Channels by PIP2 and Cholesterol.Advances in experimental medicine and biology · 2023Article
- The role of cholesterol binding in the control of cholesterol by the Scap-Insig system.European biophysics journal : EBJ · 2022Article
- The constellation of cholesterol-dependent processes associated with SARS-CoV-2 infection.Progress in lipid research · 2022Review
- Exploring TRPC3 Interaction with Cholesterol through Coarse-Grained Molecular Dynamics Simulations.Biomolecules · 2022Article
- Relative Affinities of Protein-Cholesterol Interactions from Equilibrium Molecular Dynamics Simulations.Journal of chemical theory and computation · 2021Article
- Interfacial binding sites for cholesterol on GABABiophysical journal · 2021Article
- Interfacial Binding Sites for Cholesterol on Kir, Kv, KBiophysical journal · 2020Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transient receptor potential (TRP) channels are members of a large family of ion channels located in membranes rich in cholesterol, some of whose functions are affected by the cholesterol content of the membrane. Here, cholesterol binding to TRPs is studied using a docking procedure that allows the transmembrane surface of a TRP to be swept rapidly for potential binding sites at the interfaces on the two sides of the membrane. Cholesterol docking poses determined in this way match 89% of the cholesterol hemisuccinate molecules in published TRP structures when cholesterol hemisuccinate molecules unlikely to represent typical bound cholesterols are excluded. TRPs are tetrameric, with large clefts at the interfaces between subunits; cholesterol poses are located in hollows, largely within these clefts. Comparison of cholesterol poses with phospholipid binding sites suggests that binding of cholesterol to a TRP need not result in displacement of phospholipid molecules from the TRP surface.
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Registered trials
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.