ArticleJournal of structural biology2010
Structure of the MthK RCK in complex with cadmium.
Article in Journal of structural biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
10 citing papers in PubMed.
- The allosteric gating mechanism of the MthK channel.National science review · 2022Article
- Article
- Polyamine blockade and binding energetics in the MthK potassium channel.The Journal of general physiology · 2020Article
- The pathway of transmembrane cadmium influx via calcium-permeable channels and its spatial characteristics along rice root.Journal of experimental botany · 2018Article
- Rapid cadmium SAD phasing at the standard wavelength (1 Å).Acta crystallographica. Section D, Structural biology · 2017Article
- Structural Studies of Potassium Transport Protein KtrA Regulator of Conductance of K+ (RCK) C Domain in Complex with Cyclic Diadenosine Monophosphate (c-di-AMP).The Journal of biological chemistry · 2015Article
- Initial steps of inactivation at the K+ channel selectivity filter.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Crystal structure of a Ba(2+)-bound gating ring reveals elementary steps in RCK domain activation.Structure (London, England : 1993) · 2012Article
- Structure and function of multiple Ca2+-binding sites in a K+ channel regulator of K+ conductance (RCK) domain.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- A BK (Slo1) channel journey from molecule to physiology.Channels (Austin, Tex.)Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
RCK is a cytoplasmic regulatory domain of calcium-gated potassium channels. Binding of Ca(2+) by RCK leads to channel activation through a series of yet unknown conformational changes. Structures of the K(+) channel, MthK, and its cytoplasmic RCK domain revealed two binding sites for Ca(2+) per dimer. We determined the crystal structure of RCK in complex with Cd(2+) at 2.2A resolution. Cd(2+) activates MthK more efficiently, and binds at the same binding sites for Ca(2+) but with reduced coordination number. Two additional binding sites for Cd(2+) are found per dimer; one on the main Rossman-fold lobe, and the other on the small lobe of RCK. Using patch-clamp experiments, we demonstrate that Cd(2+) binding to these novel sites enhances activation by Cd(2+) and not by Ca(2+). The structure reveals a large negatively charged surface patch in the proximity of the Ca(2+)/Cd(2+) binding sites, charge neutralization of which appears to promote the channel open state.
Indexed as
Identifiers
What OpenQuestion holds
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.