ArticleProteins2010
Cooperative nature of gating transitions in K(+) channels as seen from dynamic importance sampling calculations.
Article in Proteins, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Structural insight into the formation of lipoprotein-β-barrel complexes.Nature chemical biology · 2020Article
- Golgi anti-apoptotic proteins are highly conserved ion channels that affect apoptosis and cell migration.The Journal of biological chemistry · 2015Article
- Computational modeling of membrane proteins.Proteins · 2015Review
- Flexible gates generate occluded intermediates in the transport cycle of LacY.Journal of molecular biology · 2014Article
- Hydrophobic plug functions as a gate in voltage-gated proton channels.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Mutations in the S6 gate isolate a late step in the activation pathway and reduce 4-AP sensitivity in shaker K(v) channel.Biophysical journal · 2014Article
- The pore of voltage-gated potassium ion channels is strained when closed.Nature communications · 2013Article
- Probing the energy landscape of activation gating of the bacterial potassium channel KcsA.PLoS computational biology · 2013Article
- Towards the prediction of order parameters from molecular dynamics simulations in proteins.The Journal of chemical physics · 2012Article
- Being flexible: the voltage-controllable activation gate of kv channels.Frontiers in pharmacology · 2012Article
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Authors and funding
2 authors.
Funding
Abstract
The growing dataset of K(+) channel x-ray structures provides an excellent opportunity to begin a detailed molecular understanding of voltage-dependent gating. These structures, while differing in sequence, represent either a stable open or closed state. However, an understanding of the molecular details of gating will require models for the transitions and experimentally testable predictions for the gating transition. To explore these ideas, we apply dynamic importance sampling to a set of homology models for the molecular conformations of K(+) channels for four different sets of sequences and eight different states. In our results, we highlight the importance of particular residues upstream from the Pro-Val-Pro (PVP) region to the gating transition. This supports growing evidence that the PVP region is important for influencing the flexibility of the S6 helix and thus the opening of the gating domain. The results further suggest how gating on the molecular level depends on intra-subunit motions to influence the cooperative behavior of all four subunits of the K(+) channel. We hypothesize that the gating process occurs in steps: first sidechain movement, then inter-S5-S6 subunit motions, and lastly the large-scale domain rearrangements.
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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.