G protein-coupled receptor
From Proteopedia
(Difference between revisions)
m |
m |
||
| Line 1: | Line 1: | ||
{{Article under development}} | {{Article under development}} | ||
| - | [[G protein-coupled receptor|G protein-coupled receptors]], often abbreviated GPCRs, are an abundant superamily 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]] are cell surface signalling proteins involved in many physiological functions and in multiple diseases. they are also the target of the majority of all modern [[Pharmaceutical Drugs|medicinal drugs]] <ref name="howmany">PMID: 17139284</ref><ref name="pharmtrends">PMID: 21075459</ref>. | + | [[G protein-coupled receptor|G protein-coupled receptors]], often abbreviated GPCRs, are an abundant superamily 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]] are cell surface signalling proteins involved in many physiological functions and in multiple diseases. they are also the target of the majority of all modern [[Pharmaceutical Drugs|medicinal drugs]]<ref name="howmany">PMID: 17139284</ref><ref name="pharmtrends">PMID: 21075459</ref>. |
| + | |||
| + | The roughly 800 members of the superfamily are divided into five families of GPCRs. | ||
Rhodopsin shares similar membrane topology with the members of the superfamily (Family A of the [[G protein-coupled receptor|G protein-coupled receptors]] which include the seven transmembrane helices, an extracellular N terminus and cytoplasmic C terminus<ref name="rhodopsin">PMID:15251227</ref>. | Rhodopsin shares similar membrane topology with the members of the superfamily (Family A of the [[G protein-coupled receptor|G protein-coupled receptors]] which include the seven transmembrane helices, an extracellular N terminus and cytoplasmic C terminus<ref name="rhodopsin">PMID:15251227</ref>. | ||
| - | |||
| - | ==See Also== | ||
| - | [[Pharmaceutical Drugs]] | ||
| Line 14: | Line 13: | ||
Rhodopsins are listed individually on the [[Rhodopsin|in a section on the Rhodopsin topic page#3D structures of rhodopsin]] | Rhodopsins are listed individually on the [[Rhodopsin|in a section on the Rhodopsin topic page#3D structures of rhodopsin]] | ||
| + | |||
| + | ===Beta-2 Adrenergic Receptor=== | ||
| + | * There is a [[Beta-2 Adrenergic Receptor|topic page]]concerning the [[Beta-2 Adrenergic Receptor]] | ||
| + | * 2rh1 - human Beta 2-Adrenergic Receptor | ||
3eml | 3eml | ||
2vt4 | 2vt4 | ||
| Line 29: | Line 32: | ||
1dep | 1dep | ||
| - | [[1eds]] - solution structure of intradiskal loop 1 of bovine rhodopsin (rhodopsin residues 92-123) [[1edv]] | ||
1edw | 1edw | ||
1edx | 1edx | ||
| Line 48: | Line 50: | ||
==References and Notes== | ==References and Notes== | ||
<references/> | <references/> | ||
| + | |||
| + | ==See Also== | ||
| + | [[Pharmaceutical Drugs]] | ||
| + | [[Membrane proteins]] | ||
| + | [[Rhodopsin]] | ||
==Additional Literature== | ==Additional Literature== | ||
| Line 53: | Line 60: | ||
==External Resources== | ==External Resources== | ||
| + | * The April 2008 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Adrenergic Receptors'' by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2008_4 10.2210/rcsb_pdb/mom_2008_4]. | ||
*[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.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.cmbi.ru.nl/tinygrap/ tinyGRAP] GPCR mutant database. | ||
Revision as of 03:08, 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 superamily of proteins also known as seven-transmembrane domain receptors, 7TM receptors, heptahelical receptors, serpentine receptor, and G protein-linked receptors (GPLRs). G protein-coupled receptors are cell surface signalling proteins involved in many physiological functions and in multiple diseases. they are also the target of the majority of all modern medicinal drugs[1][2].
The roughly 800 members of the superfamily are divided into five families of GPCRs.
Rhodopsin shares similar membrane topology with the members of the superfamily (Family A of the G protein-coupled receptors which include the seven transmembrane helices, an extracellular N terminus and cytoplasmic C terminus[3].
Contents |
3D Structures of G protein-coupled receptors
Rhodopsins
Rhodopsins are listed individually on the in a section on the Rhodopsin topic page#3D structures of rhodopsin
Beta-2 Adrenergic Receptor
- There is a topic pageconcerning the Beta-2 Adrenergic Receptor
- 2rh1 - human Beta 2-Adrenergic Receptor
3eml 2vt4 2r4r 2r4s 2rh1 3d4s 3kj6 3ny8 3ny9 3nya 1bl1 1d6g 1ddv 1dep
1edw 1edx 1ewk 1ewt 1ewv 1f88 1fdf 1fjr 1gzm 1hll 1ho9 1hod 1hof 1hzn
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
- ↑ Peeters MC, van Westen GJ, Li Q, IJzerman AP. Importance of the extracellular loops in G protein-coupled receptors for ligand recognition and receptor activation. Trends Pharmacol Sci. 2011 Jan;32(1):35-42. PMID:21075459 doi:10.1016/j.tips.2010.10.001
- ↑ Kristiansen K. Molecular mechanisms of ligand binding, signaling, and regulation within the superfamily of G-protein-coupled receptors: molecular modeling and mutagenesis approaches to receptor structure and function. Pharmacol Ther. 2004 Jul;103(1):21-80. PMID:15251227 doi:10.1016/j.pharmthera.2004.05.002
See Also
Pharmaceutical Drugs Membrane proteins Rhodopsin
Additional Literature
- PMID: xxxx
External Resources
- The April 2008 RCSB PDB Molecule of the Month feature on Adrenergic Receptors by David S. Goodsell is 10.2210/rcsb_pdb/mom_2008_4.
- 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.
Proteopedia Page Contributors and Editors (what is this?)
Alexander Berchansky, Wayne Decatur, Michal Harel, Ann Taylor, Nikki Hunter
