ATP binding site on the C-terminus of the vanilloid receptor
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
17706589
DOI
10.1016/j.abb.2007.06.035
PII: S0003-9861(07)00339-6
Knihovny.cz E-resources
- MeSH
- Adenosine Triphosphate analogs & derivatives chemistry MeSH
- Models, Chemical * MeSH
- TRPV Cation Channels chemistry ultrastructure MeSH
- Protein Conformation MeSH
- Models, Molecular * MeSH
- Computer Simulation MeSH
- Protein Binding MeSH
- Binding Sites MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- 2',3'-O-(2,4,6-trinitro-cyclohexadienylidine)adenosine 5'-triphosphate MeSH Browser
- Adenosine Triphosphate MeSH
- TRPV Cation Channels MeSH
- TRPV1 receptor MeSH Browser
Transient receptor potential channel vanilloid receptor subunit 1 (TRPV1) is a thermosensitive cation channel activated by noxious heat as well as a wide range of chemical stimuli. Although ATP by itself does not directly activate TRPV1, it was shown that intracellular ATP increases its activity by directly interacting with the Walker A motif residing on the C-terminus of TRPV1. In order to identify the amino acid residues that are essential for the binding of ATP to the TRPV1 channel, we performed the following point mutations of the Walker A motif: P732A, D733A, G734A, K735A, D736A, and D737A. Employing bulk fluorescence measurements, namely a TNP-ATP competition assay and FITC labelling and quenching experiments, we identified the key role of the K735 residue in the binding of the nucleotide. Experimental data was interpreted according to our molecular modelling simulations.
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