期刊
STRUCTURE
卷 13, 期 8, 页码 1203-1211出版社
CELL PRESS
DOI: 10.1016/j.str.2005.06.005
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资金
- NCRR NIH HHS [P41RR02250, P41 RR002250] Funding Source: Medline
- NIAMS NIH HHS [R01AR44864, R01AR41729, R01 AR044864, R01 AR041729] Funding Source: Medline
- NIGMS NIH HHS [R01 GM072804-02, P01GM99116, R01 GM072804-01, R01 GM072804-03, R01GM072804, R01 GM072804-05S1, R01 GM072804-05, R01 GM072804, R01 GM072804-04] Funding Source: Medline
Using single particle electron cryomicroscopy, several helices in the membrane-spanning region of RyR1, including an inner transmembrane helix, a short pore helix, and a helix parallel to the membrane on the cytoplasmic side, have been clearly resolved. Our model places a highly conserved glycine (G4934) at the hinge position of the bent inner helix and two rings of negative charges at the luminal and cytoplasmic mouths of the pore. The kinked inner helix closely resembles the inner helix of the open MthK channel, suggesting that kinking alone does not open RyR1, as proposed for K channels.
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