ArticleBiophysical journal2006
Three-dimensional visualization of FKBP12.6 binding to an open conformation of cardiac ryanodine receptor.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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
24 citing papers in PubMed, 54 citations in OpenAlex.
- Cryo-EM Brings the Mechanisms of Activation, Inactivation, and Inhibition of Ryanodine Receptors into Focus.Advances in experimental medicine and biology · 2026Review
- Synchronizing systolic calcium release with azumolene in an experimental model.Heart rhythm O2 · 2022Article
- The FKBP12 subunit modifies the long-range allosterism of the ryanodine receptor.Journal of structural biology · 2019Article
- The structural basis of ryanodine receptor ion channel function.The Journal of general physiology · 2017Review
- A guide to the 3D structure of the ryanodine receptor type 1 by cryoEM.Protein science : a publication of the Protein Society · 2017Review
- Current topics in catecholaminergic polymorphic ventricular tachycardia.Journal of arrhythmia · 2016Review
- Ultrastructural Analysis of Self-Associated RyR2s.Biophysical journal · 2016Article
- Crystal structures of ryanodine receptor SPRY1 and tandem-repeat domains reveal a critical FKBP12 binding determinant.Nature communications · 2015Article
- FKBP12.6 activates RyR1: investigating the amino acid residues critical for channel modulation.Biophysical journal · 2014Article
- Structure of glutaraldehyde cross-linked ryanodine receptor.Journal of structural biology · 2013Article
- Ligand-dependent conformational changes in the clamp region of the cardiac ryanodine receptor.The Journal of biological chemistry · 2013Article
- Modeling a ryanodine receptor N-terminal domain connecting the central vestibule and the corner clamp region.The Journal of biological chemistry · 2013Article
- Altered sarcoplasmic reticulum calcium cycling--targets for heart failure therapy.Nature reviews. Cardiology · 2012Review
- The role of FK506-binding proteins 12 and 12.6 in regulating cardiac function.Pediatric cardiology · 2012Article
- Article
- FKBP12 activates the cardiac ryanodine receptor Ca2+-release channel and is antagonised by FKBP12.6.PloS one · 2012Article
- Localization of the dantrolene-binding sequence near the FK506-binding protein-binding site in the three-dimensional structure of the ryanodine receptor.The Journal of biological chemistry · 2011Article
- Ryanodine receptors: structure, expression, molecular details, and function in calcium release.Cold Spring Harbor perspectives in biology · 2010Review
- Mapping the ryanodine receptor FK506-binding protein subunit using fluorescence resonance energy transfer.The Journal of biological chemistry · 2010Article
- Dynamic, inter-subunit interactions between the N-terminal and central mutation regions of cardiac ryanodine receptor.Journal of cell science · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
The cardiac isoform of the ryanodine receptor (RyR2) from dog binds predominantly a 12.6-kDa isoform of the FK506-binding protein (FKBP12.6), whereas RyR2 from other species binds both FKBP12.6 and the closely related isoform FKBP12. The role played by FKBP12.6 in modulating calcium release by RyR2 is unclear at present. We have used cryoelectron microscopy and three-dimensional (3D) reconstruction techniques to determine the binding position of FKBP12.6 on the surface of canine RyR2. Buffer conditions that should favor the "open" state of RyR2 were used. Quantitative comparison of 3D reconstructions of RyR2 in the presence and absence of FKBP12.6 reveals that FKBP12.6 binds along the sides of the square-shaped cytoplasmic region of the receptor, adjacent to domain 9, which forms part of the four clamp (corner-forming) structures. The location of the FKBP12.6 binding site on "open" RyR2 appears similar, but slightly displaced (by 1-2 nm) from that found previously for FKBP12 binding to the skeletal muscle ryanodine receptor that was in the buffer that favors the "closed" state. The conformation of RyR2 containing bound FKBP12.6 differs considerably from that depleted of FKBP12.6, particularly in the transmembrane region and in the clamp structures. The x-ray structure of FKBP12.6 was docked into the region of the 3D reconstruction that is attributable to bound FKBP12.6, to show the relative orientations of amino acid residues (Gln-31, Asn-32, Phe-59) that have been implicated as being critical in interactions with RyR2. A thorough understanding of the structural basis of RyR2-FKBP12.6 interaction should aid in understanding the roles that have been proposed for FKBP12.6 in heart failure and in certain forms of sudden cardiac death.
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.