Abstract
We used a combination of bioinformatics, electron cryomicroscopy, and biochemical techniques to identify an oxidoreductase-like domain in the skeletal muscle Ca2+ release channel protein (RyR1). The initial prediction was derived from sequence-based fold recognition for the N-terminal region (41-420) of RyR1. The putative domain was computationally localized to the clamp domain in the cytoplasmic region of a 22A structure of RyR1. This localization was subsequently confirmed by difference imaging with a sequence specific antibody. Consistent with the prediction of an oxidoreductase domain, RyR1 binds [3H]NAD+, supporting a model in which RyR1 has a oxidoreductase-like domain that could function as a type of redox sensor.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Biophysical Phenomena
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Biophysics
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Computer Simulation
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Cryoelectron Microscopy
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In Vitro Techniques
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Models, Molecular
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Molecular Sequence Data
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Muscle, Skeletal / metabolism
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NAD / metabolism
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Oxidation-Reduction
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Oxidoreductases / chemistry*
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Oxidoreductases / genetics
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Oxidoreductases / metabolism
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Protein Structure, Tertiary
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Rabbits
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Ryanodine Receptor Calcium Release Channel / chemistry*
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Ryanodine Receptor Calcium Release Channel / genetics
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Ryanodine Receptor Calcium Release Channel / metabolism
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Sequence Homology, Amino Acid
Substances
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Ryanodine Receptor Calcium Release Channel
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NAD
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Oxidoreductases