Structural highlights
Publication Abstract from PubMed
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.
Apo and InsP(3)-bound crystal structures of the ligand-binding domain of an InsP(3) receptor.,Lin CC, Baek K, Lu Z Nat Struct Mol Biol. 2011 Sep 4. doi: 10.1038/nsmb.2112. PMID:21892169[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lin CC, Baek K, Lu Z. Apo and InsP(3)-bound crystal structures of the ligand-binding domain of an InsP(3) receptor. Nat Struct Mol Biol. 2011 Sep 4. doi: 10.1038/nsmb.2112. PMID:21892169 doi:10.1038/nsmb.2112
