Skip Navigation


PEDS Advance Access originally published online on March 24, 2006
Protein Engineering Design and Selection 2006 19(6):277-283; doi:10.1093/protein/gzl010
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow All Versions of this Article:
19/6/277    most recent
gzl010v1
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 (2)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Muramatsu, T.
Right arrow Articles by Suwa, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Muramatsu, T.
Right arrow Articles by Suwa, M.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author 2006. Published by Oxford University Press. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

Statistical analysis and prediction of functional residues effective for GPCR–G-protein coupling selectivity

Takahiko Muramatsu1,2,3 and Makiko Suwa1,2

1 Graduate School of Information Science, Nara Institute of Science and Technology (NAIST) 8915-5 Takayama, Ikoma, Nara 630-1010, Japan 2 Computational Biology Research Center (CBRC), National Institute of Advanced Industrial Science and Technology (AIST) AIST Waterfront BIO-IT Research Building, 2-42 Aomi, Koto-ku, Tokyo 135-0064, Japan

3To whom correspondence should be addressed. E-mail: taka-mu{at}is.naist.jp

One of the important issues in G-protein-coupled receptor (GPCR) functional analysis is the mechanism of GPCR–G-protein coupling selectivity. G-proteins are classified into Gi/o, Gq/11 and Gs families. Although several experimental and computational analyses have been attempted, the mechanism remains unknown to this day. In this study, we have analyzed the multiple sequence alignments of GPCRs of known coupling selectivities by mapping onto the tertiary structure of rhodopsin. We identified several functional residue sites in GPCRs related to coupling selectivity, which are located mainly at the intracellular loops, and found that the occurrence of positively/negatively charged amino acids of the characteristic residues varies depending on the G-protein coupling selectivity. Especially, the occurrence of positively charged amino acids in receptors coupling to Gs family is less than that in receptors coupling to Gi/o and Gq/11 families. It is interesting that some characteristic residues are located near the extracellular terminus of transmembrane helices, which is far from the GPCR/G-protein binding interface. In most of the receptors coupling to Gs family, the occurrence of proline on the position corresponding to the 170th residue on rhodopsin is rare. These findings are vital to improving our understanding of the mechanism of G-protein coupling selectivity.

Keywords: G-protein-coupled receptor/functional residue site/correlation coefficient/rhodopsin/protein-protein interaction

Received September 6, 2005; revised January 17, 2006; accepted February 20, 2006.

Edited by Mark Sansom


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




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.