Structural highlights
Function
[ITPR1_RAT] Intracellular channel that mediates calcium release from the endoplasmic reticulum following stimulation by inositol 1,4,5-trisphosphate. Plays a role in ER stress-induced apoptosis. Cytoplasmic calcium released from the ER triggers apoptosis by the activation of CaM kinase II, eventually leading to the activation of downstream apoptosis pathways (By similarity).
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
