Entropy and oligomerization in GPCRs
- PMID: 16012184
- DOI: 10.1385/JMN:26:2-3:113
Entropy and oligomerization in GPCRs
Abstract
Evolutionary trace (ET) and entropy are two related methods for analyzing a multiple sequence alignment to determine functionally important residues in proteins. In this article, these methods have been enhanced with a view to reinvestigate the issue ofGPCR dimerization and oligomerization. In particular, cluster analysis has replaced the subjective visual analysis element of the original ET method. Previous applications of the ET method predicted two dimerization interfaces on the external transmembrane lipid-facing region of GPCRs; these were discussed in terms of dimerization and linear oligomers. Removing the subjective element of the ET method gives rise to the prediction of functionally important residues on the external face of each transmembrane helix for a large number of class A GPCRs. These results are consistent with a growing body of experimental information that, taken over many receptor subtypes, has implicated each transmembrane helix in dimeric interactions. In this application, entropy gave superior results to those obtained from the ET method in that its use gives rise to higher z-scores and fewer instances of z-scores below 3.
Similar articles
-
Computational studies of Family A and Family B GPCRs.Biochem Soc Trans. 2007 Aug;35(Pt 4):749-54. doi: 10.1042/BST0350749. Biochem Soc Trans. 2007. PMID: 17635140 Review.
-
The study of G-protein coupled receptor oligomerization with computational modeling and bioinformatics.FEBS J. 2005 Jun;272(12):2926-38. doi: 10.1111/j.1742-4658.2005.04730.x. FEBS J. 2005. PMID: 15955053 Review.
-
A two-entropies analysis to identify functional positions in the transmembrane region of class A G protein-coupled receptors.Proteins. 2006 Jun 1;63(4):1018-30. doi: 10.1002/prot.20899. Proteins. 2006. PMID: 16532452
-
Statistical sequence analyses of G-protein-coupled receptors: structural and functional characteristics viewed with periodicities of entropy, hydrophobicity, and volume.Proteins. 2004 Sep 1;56(4):650-60. doi: 10.1002/prot.20068. Proteins. 2004. PMID: 15281118
-
Dimerization in aminergic G-protein-coupled receptors: application of a hidden-site class model of evolution.Biochemistry. 2003 Dec 16;42(49):14522-31. doi: 10.1021/bi035097r. Biochemistry. 2003. PMID: 14661965
Cited by
-
Modulation of adenosine A2a receptor oligomerization by receptor activation and PIP2 interactions.Structure. 2021 Nov 4;29(11):1312-1325.e3. doi: 10.1016/j.str.2021.06.015. Epub 2021 Jul 15. Structure. 2021. PMID: 34270937 Free PMC article.
-
Inactive and active states and supramolecular organization of GPCRs: insights from computational modeling.J Comput Aided Mol Des. 2006 Jul-Aug;20(7-8):449-61. doi: 10.1007/s10822-006-9064-0. Epub 2006 Sep 29. J Comput Aided Mol Des. 2006. PMID: 17009093 Review.
-
Theoretical considerations on the topological organization of receptor mosaics.Curr Protein Pept Sci. 2009 Dec;10(6):559-69. doi: 10.2174/138920309789630606. Curr Protein Pept Sci. 2009. PMID: 19751189 Free PMC article. Review.
-
Identification of Small-Molecule Positive Modulators of Calcitonin-like Receptor-Based Receptors.ACS Pharmacol Transl Sci. 2020 Mar 12;3(2):305-320. doi: 10.1021/acsptsci.9b00108. eCollection 2020 Apr 10. ACS Pharmacol Transl Sci. 2020. PMID: 32296770 Free PMC article.
-
Quaternary structure predictions of transmembrane proteins starting from the monomer: a docking-based approach.BMC Bioinformatics. 2006 Jul 12;7:340. doi: 10.1186/1471-2105-7-340. BMC Bioinformatics. 2006. PMID: 16836758 Free PMC article.
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources