ArticleJournal of molecular modeling2013
Targeted molecular dynamics (TMD) of the full-length KcsA potassium channel: on the role of the cytoplasmic domain in the opening process.
Article in Journal of molecular modeling, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Unveiling the Gating Mechanism of CRAC Channel: A Computational Study.Frontiers in molecular biosciences · 2021Article
- Acidic pH sensing in the bacterial cytoplasm is required for Salmonella virulence.Molecular microbiology · 2016Article
- Molecular modeling study of the induced-fit effect on kinase inhibition: the case of fibroblast growth factor receptor 3 (FGFR3).Journal of computer-aided molecular design · 2015Article
- Identification of the Conformational transition pathway in PIP2 Opening Kir Channels.Scientific reports · 2015Article
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Authors and funding
5 authors.
Funding
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Abstract
Some recent papers clearly indicate that the cytoplasmic domain of KcsA plays a role in pH sensing. We have performed, for the first time, a targeted molecular dynamics (TMD) simulation of the opening of full-length KcsA at pH 4 and pH 7, with a special interest for the cytoplasmic domain. Association energy calculations show a stabilization at pH 7 confirming that the protonation of some amino-acids at pH 4 in this domain plays a role in the opening process. A careful analysis of the pH dependent charges borne by residues in the cytoplasmic domain and their interactions confirms some literature experimental data and permits to give further insight into the role played by some of them in the opening process.
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