G protein-coupled receptor
From Proteopedia
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[[G protein-coupled receptor|G protein-coupled receptors]], often abbreviated GPCRs, are an abundant class of proteins also known as [[G protein-coupled receptor|seven-transmembrane domain receptors]], [[G protein-coupled receptor|7TM receptors]], [[G protein-coupled receptor|heptahelical receptors]], [[G protein-coupled receptor|serpentine receptor]], and [[G protein-coupled receptor|G protein-linked receptors (GPLRs)]]. | [[G protein-coupled receptor|G protein-coupled receptors]], often abbreviated GPCRs, are an abundant class of proteins also known as [[G protein-coupled receptor|seven-transmembrane domain receptors]], [[G protein-coupled receptor|7TM receptors]], [[G protein-coupled receptor|heptahelical receptors]], [[G protein-coupled receptor|serpentine receptor]], and [[G protein-coupled receptor|G protein-linked receptors (GPLRs)]]. | ||
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| + | [[G protein-coupled receptor|G protein-coupled receptors] are involved in many diseases, and are also the target of approximately 30% of all modern medicinal drugs <ref name="howmany">PMID: 17139284</ref>. | ||
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| + | ==See Also== | ||
| + | [[Pharmaceutical Drugs]] | ||
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| + | ==3D Structures of G protein-coupled receptors== | ||
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| + | ==References and Notes== | ||
| + | <references/> | ||
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| + | ==Additional Literature== | ||
| + | <ref group="xtra">PMID: 18420935</ref><ref group="xtra">PMID: 16720699 </ref><ref group="xtra">PMID: 18332149</ref><ref group="xtra">PMID: 19535337</ref><ref group="xtra">PMID: 19595807</ref><ref group="xtra">PMID: 19728889 </ref><ref group="xtra">PMID: 20141420</ref><ref group="xtra">PMID: 17517123</ref><ref group="xtra">PMID: 19627256</ref><ref group="xtra">PMID: 15961631</ref><ref group="xtra">PMID: 20084417</ref><ref group="xtra">PMID: 18701082</ref><references group="xtra"/> | ||
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| + | ==External Resources== | ||
| + | *[http://www.gpcr.org/7tm/ GPCRDB: database contains sequences, ligand binding constants and mutations, in addition GPCR multiple sequence alignments and homology models]. Moreover, the site contains useful structure files where lysozyme and other inserts commonly used in the difficult process of [[X-ray crystallography|crystallizing]] these transmembrane structures are removed. | ||
| + | * [http://www.cmbi.ru.nl/tinygrap/ tinyGRAP] GPCR mutant database. | ||
| + | * [http://www.gpcr-okb.org/ GPCR-OKB: GPCR Oligomerization Knowledge Base] | ||
| + | * [http://nava.liacs.nl/ GPCR Natural Variants Database (NaVa)] | ||
| + | * [http://athina.biol.uoa.gr/bioinformatics/PRED-GPCR/ The PRED-GPCR server] for GPCR recognition and family classification. | ||
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| + | [[Category:Topic Page]] | ||
Revision as of 01:38, 7 September 2011
| For the date when the most recent work on this article was done, click on the history tab above. |
G protein-coupled receptors, often abbreviated GPCRs, are an abundant class of proteins also known as seven-transmembrane domain receptors, 7TM receptors, heptahelical receptors, serpentine receptor, and G protein-linked receptors (GPLRs).
[[G protein-coupled receptor|G protein-coupled receptors] are involved in many diseases, and are also the target of approximately 30% of all modern medicinal drugs [1].
Contents |
See Also
3D Structures of G protein-coupled receptors
References and Notes
- ↑ Overington JP, Al-Lazikani B, Hopkins AL. How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. PMID:17139284 doi:10.1038/nrd2199
Additional Literature
- Liu L, Botos I, Wang Y, Leonard JN, Shiloach J, Segal DM, Davies DR. Structural basis of toll-like receptor 3 signaling with double-stranded RNA. Science. 2008 Apr 18;320(5874):379-81. PMID:18420935 doi:320/5874/379
- Bell JK, Askins J, Hall PR, Davies DR, Segal DM. The dsRNA binding site of human Toll-like receptor 3. Proc Natl Acad Sci U S A. 2006 Jun 6;103(23):8792-7. Epub 2006 May 23. PMID:16720699 doi:10.1073/pnas.0603245103
- Nyman T, Stenmark P, Flodin S, Johansson I, Hammarstrom M, Nordlund P. The crystal structure of the human toll-like receptor 10 cytoplasmic domain reveals a putative signaling dimer. J Biol Chem. 2008 May 2;283(18):11861-5. Epub 2008 Mar 10. PMID:18332149 doi:10.1074/jbc.C800001200
- Chan SL, Low LY, Hsu S, Li S, Liu T, Santelli E, Le Negrate G, Reed JC, Woods VL Jr, Pascual J. Molecular mimicry in innate immunity: crystal structure of a bacterial TIR domain. J Biol Chem. 2009 Aug 7;284(32):21386-92. Epub 2009 Jun 17. PMID:19535337 doi:10.1074/jbc.C109.007591
- Botos I, Liu L, Wang Y, Segal DM, Davies DR. The toll-like receptor 3:dsRNA signaling complex. Biochim Biophys Acta. 2009 Sep-Oct;1789(9-10):667-74. Epub 2009 Jul 9. PMID:19595807 doi:10.1016/j.bbagrm.2009.06.005
- Istomin AY, Godzik A. Understanding diversity of human innate immunity receptors: analysis of surface features of leucine-rich repeat domains in NLRs and TLRs. BMC Immunol. 2009 Sep 3;10:48. PMID:19728889 doi:10.1186/1471-2172-10-48
- Satake H, Sasaki N. Comparative overview of toll-like receptors in lower animals. Zoolog Sci. 2010 Feb;27(2):154-61. PMID:20141420 doi:10.2108/zsj.27.154
- Matsushima N, Tanaka T, Enkhbayar P, Mikami T, Taga M, Yamada K, Kuroki Y. Comparative sequence analysis of leucine-rich repeats (LRRs) within vertebrate toll-like receptors. BMC Genomics. 2007 May 21;8:124. PMID:17517123 doi:10.1186/1471-2164-8-124
- Carpenter S, O'Neill LA. Recent insights into the structure of Toll-like receptors and post-translational modifications of their associated signalling proteins. Biochem J. 2009 Jul 29;422(1):1-10. PMID:19627256 doi:10.1042/BJ20090616
- Choe J, Kelker MS, Wilson IA. Crystal structure of human toll-like receptor 3 (TLR3) ectodomain. Science. 2005 Jul 22;309(5734):581-5. Epub 2005 Jun 16. PMID:15961631
- Gong J, Wei T, Zhang N, Jamitzky F, Heckl WM, Rossle SC, Stark RW. TollML: a database of toll-like receptor structural motifs. J Mol Model. 2010 Jul;16(7):1283-9. Epub 2010 Jan 19. PMID:20084417 doi:10.1007/s00894-009-0640-9
- Jin MS, Lee JO. Structures of the toll-like receptor family and its ligand complexes. Immunity. 2008 Aug 15;29(2):182-91. PMID:18701082 doi:10.1016/j.immuni.2008.07.007
External Resources
- GPCRDB: database contains sequences, ligand binding constants and mutations, in addition GPCR multiple sequence alignments and homology models. Moreover, the site contains useful structure files where lysozyme and other inserts commonly used in the difficult process of crystallizing these transmembrane structures are removed.
- tinyGRAP GPCR mutant database.
- GPCR-OKB: GPCR Oligomerization Knowledge Base
- GPCR Natural Variants Database (NaVa)
- The PRED-GPCR server for GPCR recognition and family classification.
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