|Title||Conformational motions and ligand-binding underlying gating and regulation in IPR channel.|
|Journal, issue, pages||Nat Commun, Vol. 13, Issue 1, Page 6942, Year 2022|
|Publish date||Nov 14, 2022|
|Authors||Guizhen Fan / Mariah R Baker / Lara E Terry / Vikas Arige / Muyuan Chen / Alexander B Seryshev / Matthew L Baker / Steven J Ludtke / David I Yule / Irina I Serysheva /|
|PubMed Abstract||Inositol-1,4,5-trisphosphate receptors (IPRs) are activated by IP and Ca and their gating is regulated by various intracellular messengers that finely tune the channel activity. Here, using single ...Inositol-1,4,5-trisphosphate receptors (IPRs) are activated by IP and Ca and their gating is regulated by various intracellular messengers that finely tune the channel activity. Here, using single particle cryo-EM analysis we determined 3D structures of the nanodisc-reconstituted IPR1 channel in two ligand-bound states. These structures provide unprecedented details governing binding of IP, Ca and ATP, revealing conformational changes that couple ligand-binding to channel opening. Using a deep-learning approach and 3D variability analysis we extracted molecular motions of the key protein domains from cryo-EM density data. We find that IP binding relies upon intrinsic flexibility of the ARM2 domain in the tetrameric channel. Our results highlight a key role of dynamic side chains in regulating gating behavior of IPR channels. This work represents a stepping-stone to developing mechanistic understanding of conformational pathways underlying ligand-binding, activation and regulation of the channel.|
|External links||Nat Commun / PubMed:36376291 / PubMed Central|
|Methods||EM (single particle)|
|Resolution||3.26 - 3.5 Å|
|Keywords||MEMBRANE PROTEIN / Calcium channel / lipid nanodisc|
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