3t8s | pdb_00003t8s
From Proteopedia
Apo and InsP3-bound Crystal Structures of the Ligand-Binding Domain of an InsP3 Receptor
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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 PubMedWe 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 AlsoReferences
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This page was last modified 11:15, 10 December 2016.