Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (16)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Shah, P. K.
Right arrow Articles by Sowdhamini, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Shah, P. K.
Right arrow Articles by Sowdhamini, R.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Protein Engineering, Vol. 14, No. 11, 867-874, November 2001
© 2001 Oxford University Press

Structural understanding of the transmembrane domains of inositol triphosphate receptors and ryanodine receptors towards calcium channeling

Parantu K. Shah and R. Sowdhamini,1

National Centre for Biological Sciences, Tata Institute of Fundamental Research, GKVK Campus, Bangalore 560 065, India

Inositol 1,4,5-triphosphate receptors (Insp3Rs) and ryanodine receptors (ryRs) act as cationic channels transporting calcium ions from the endoplasmic reticulum to cytosol by forming tetramers and are proteins localized to the endoplasmic reticulum (ER). Despite the absence of classical calcium-binding motifs, calcium channeling occurs at the transmembrane domain. We have investigated putative calcium binding motifs in these sequences. Prediction methods indicate the presence of six transmembrane helices in the C-terminal domain, one of the three domains conserved between Insp3R and ryR receptors. The recently identified crystal structure of the K+ channel, which also forms tetramers, revealed that two transmembrane helices, an additional pore helix and a selectivity filter are responsible for selective K+ ion channeling. The last three TM helices of Insp3R and ryR are particularly well conserved and we found analogous pore helix and selectivity filter motif in these sequences. We obtained a three-dimensional structural model for the transmembrane tetramer by extrapolating the distant structural similarity to the K+ channels.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Physiol. Rev.Home page
J. K. Foskett, C. White, K.-H. Cheung, and D.-O. D. Mak
Inositol Trisphosphate Receptor Ca2+ Release Channels
Physiol Rev, April 1, 2007; 87(2): 593 - 658.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Pharmacol.Home page
K. M. Ranatunga, T. M. Moreno-King, B. Tanna, R. Wang, S. R. W. Chen, L. Ruest, W. Welch, and A. J. Williams
The Gln4863Ala Mutation within a Putative, Pore-Lining Trans-Membrane Helix of the Cardiac Ryanodine Receptor Channel Alters Both the Kinetics of Ryanoid Interaction and the Subsequent Fractional Conductance
Mol. Pharmacol., September 1, 2005; 68(3): 840 - 846.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. Hamada, A. Terauchi, and K. Mikoshiba
Three-dimensional Rearrangements within Inositol 1,4,5-Trisphosphate Receptor by Calcium
J. Biol. Chem., December 26, 2003; 278(52): 52881 - 52889.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
G. I. Anyatonwu, E. D. Buck, and B. E. Ehrlich
Methanethiosulfonate Ethylammonium Block of Amine Currents through the Ryanodine Receptor Reveals Single Pore Architecture
J. Biol. Chem., November 14, 2003; 278(46): 45528 - 45538.
[Abstract] [Full Text] [PDF]

Home page
 Physiol. Rev.Home page
M. Fill and J. A. Copello
Ryanodine Receptor Calcium Release Channels
Physiol Rev, October 1, 2002; 82(4): 893 - 922.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.