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Apo and InsP(3)-bound crystal structures of the ligand-binding domain of an InsP(3) receptor
We report the crystal structures of the ligand-binding domain (LBD) of a rat inositol 1,4,5-trisphosphate (InsP(3)) 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 (AR...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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2011
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3242432/ https://www.ncbi.nlm.nih.gov/pubmed/21892169 http://dx.doi.org/10.1038/nsmb.2112 |
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author | Lin, Chun-Chi Baek, Kyuwon Lu, Zhe |
author_facet | Lin, Chun-Chi Baek, Kyuwon Lu, Zhe |
author_sort | Lin, Chun-Chi |
collection | PubMed |
description | We report the crystal structures of the ligand-binding domain (LBD) of a rat inositol 1,4,5-trisphosphate (InsP(3)) 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 towards the active state. |
format | Online Article Text |
id | pubmed-3242432 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
record_format | MEDLINE/PubMed |
spelling | pubmed-32424322012-04-01 Apo and InsP(3)-bound crystal structures of the ligand-binding domain of an InsP(3) receptor Lin, Chun-Chi Baek, Kyuwon Lu, Zhe Nat Struct Mol Biol Article We report the crystal structures of the ligand-binding domain (LBD) of a rat inositol 1,4,5-trisphosphate (InsP(3)) 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 towards the active state. 2011-09-04 /pmc/articles/PMC3242432/ /pubmed/21892169 http://dx.doi.org/10.1038/nsmb.2112 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms |
spellingShingle | Article Lin, Chun-Chi Baek, Kyuwon Lu, Zhe Apo and InsP(3)-bound crystal structures of the ligand-binding domain of an InsP(3) receptor |
title | Apo and InsP(3)-bound crystal structures of the ligand-binding domain of an InsP(3) receptor |
title_full | Apo and InsP(3)-bound crystal structures of the ligand-binding domain of an InsP(3) receptor |
title_fullStr | Apo and InsP(3)-bound crystal structures of the ligand-binding domain of an InsP(3) receptor |
title_full_unstemmed | Apo and InsP(3)-bound crystal structures of the ligand-binding domain of an InsP(3) receptor |
title_short | Apo and InsP(3)-bound crystal structures of the ligand-binding domain of an InsP(3) receptor |
title_sort | apo and insp(3)-bound crystal structures of the ligand-binding domain of an insp(3) receptor |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3242432/ https://www.ncbi.nlm.nih.gov/pubmed/21892169 http://dx.doi.org/10.1038/nsmb.2112 |
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