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PDBsum entry 5j8v
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Transport protein
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PDB id
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5j8v
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PDB id:
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| Name: |
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Transport protein
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Title:
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Structure of rabbit ryanodine receptor ryr1 open state activated by calcium ion
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Structure:
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Ryanodine receptor 1. Chain: a, b, c, d. Synonym: ryr1,skeletal muscle calcium release channel,skeletal muscle ryanodine receptor,skeletal muscle-type ryanodine receptor,type 1 ryanodine receptor
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Source:
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Oryctolagus cuniculus. Rabbit. Organism_taxid: 9986
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Authors:
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X.Wang,R.Wei,C.Yin,F.Sun
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Key ref:
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R.Wei
et al.
(2016).
Structural insights into Ca(2+)-activated long-range allosteric channel gating of RyR1.
Cell Res,
26,
977-994.
PubMed id:
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Date:
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08-Apr-16
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Release date:
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14-Sep-16
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PROCHECK
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Headers
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References
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P11716
(RYR1_RABIT) -
Ryanodine receptor 1 from Oryctolagus cuniculus
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Seq:
Struc:
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5037 a.a.
3453 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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Cell Res
26:977-994
(2016)
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PubMed id:
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Structural insights into Ca(2+)-activated long-range allosteric channel gating of RyR1.
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R.Wei,
X.Wang,
Y.Zhang,
S.Mukherjee,
L.Zhang,
Q.Chen,
X.Huang,
S.Jing,
C.Liu,
S.Li,
G.Wang,
Y.Xu,
S.Zhu,
A.J.Williams,
F.Sun,
C.C.Yin.
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ABSTRACT
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Ryanodine receptors (RyRs) are a class of giant ion channels with molecular mass
over 2.2 mega-Daltons. These channels mediate calcium signaling in a variety of
cells. Since more than 80% of the RyR protein is folded into the cytoplasmic
assembly and the remaining residues form the transmembrane domain, it has been
hypothesized that the activation and regulation of RyR channels occur through an
as yet uncharacterized long-range allosteric mechanism. Here we report the
characterization of a Ca(2+)-activated open-state RyR1 structure by
cryo-electron microscopy. The structure has an overall resolution of 4.9 Å and
a resolution of 4.2 Å for the core region. In comparison with the previously
determined apo/closed-state structure, we observed long-range allosteric gating
of the channel upon Ca(2+) activation. In-depth structural analyses elucidated a
novel channel-gating mechanism and a novel ion selectivity mechanism of RyR1.
Our work not only provides structural insights into the molecular mechanisms of
channel gating and regulation of RyRs, but also sheds light on structural basis
for channel-gating and ion selectivity mechanisms for the
six-transmembrane-helix cation channel family.
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Links
