ArticlePloS one2011
3D Mapping of the SPRY2 domain of ryanodine receptor 1 by single-particle cryo-EM.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed.
- TRIC-A Channel Maintains Store Calcium Handling by Interacting With Type 2 Ryanodine Receptor in Cardiac Muscle.Circulation research · 2020Article
- CaTrends in biochemical sciences · 2017Review
- A guide to the 3D structure of the ryanodine receptor type 1 by cryoEM.Protein science : a publication of the Protein Society · 2017Review
- While the revolution will not be crystallized, biochemistry reigns supreme.Protein science : a publication of the Protein Society · 2017Review
- Structure of the SPRY domain of the human RNA helicase DDX1, a putative interaction platform within a DEAD-box protein.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Germline mutations in RYR1 are associated with foetal akinesia deformation sequence/lethal multiple pterygium syndrome.Acta neuropathologica communications · 2014Article
- Structure of glutaraldehyde cross-linked ryanodine receptor.Journal of structural biology · 2013Article
- Subunit organization of a synechocystis hetero-oligomeric thylakoid FtsH complex involved in photosystem II repair.The Plant cell · 2012Article
- Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The type 1 skeletal muscle ryanodine receptor (RyR1) is principally responsible for Ca(2+) release from the sarcoplasmic reticulum and for the subsequent muscle contraction. The RyR1 contains three SPRY domains. SPRY domains are generally known to mediate protein-protein interactions, however the location of the three SPRY domains in the 3D structure of the RyR1 is not known. Combining immunolabeling and single-particle cryo-electron microscopy we have mapped the SPRY2 domain (S1085-V1208) in the 3D structure of RyR1 using three different antibodies against the SPRY2 domain. Two obstacles for the image processing procedure; limited amount of data and signal dilution introduced by the multiple orientations of the antibody bound in the tetrameric RyR1, were overcome by modifying the 3D reconstruction scheme. This approach enabled us to ascertain that the three antibodies bind to the same region, to obtain a 3D reconstruction of RyR1 with the antibody bound, and to map SPRY2 to the periphery of the cytoplasmic domain of RyR1. We report here the first 3D localization of a SPRY2 domain in any known RyR isoform.
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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.