Format

Send to

Choose Destination
See comment in PubMed Commons below
Nat Struct Mol Biol. 2011 Sep 4;18(10):1172-4. doi: 10.1038/nsmb.2112.

Apo and InsP₃-bound crystal structures of the ligand-binding domain of an InsP₃ receptor.

Author information

1
Department of Physiology, Howard Hughes Medical Institute, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, USA.

Abstract

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 β-trefoil fold (β-TF1) and armadillo repeat fold (ARF) move together as a unit relative to its second β-trefoil fold (β-TF2). Whereas apo LBD may spontaneously transition between gating conformations, InsP(3) binding shifts this equilibrium toward the active state.

PMID:
21892169
PMCID:
PMC3242432
DOI:
10.1038/nsmb.2112
[Indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Nature Publishing Group Icon for PubMed Central
    Loading ...
    Support Center