期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 18, 期 10, 页码 1172-1174出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2112
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资金
- Howard Hughes Medical Institute
We report the crystal structures of the ligand-binding domain (LBD) of a rat inositol 1,4,5-trisphosphate receptor (InsP(3)R) in its apo and InsP(3)-bound conformations. Comparison of these two conformations reveals that LBD's first beta-trefoil fold (beta-TF1) and armadillo repeat fold (ARF) move together as a unit relative to its second beta-trefoil fold (beta-TF2). Whereas apo LBD may spontaneously transition between gating conformations, InsP(3) binding shifts this equilibrium toward the active state.
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