Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 18, Issue 10, Pages 1172-1174Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2112
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Funding
- Howard Hughes Medical Institute
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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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