NDLI: The fourth intracellular domain of G-protein coupling receptors: helicity, basicity and similarity to opsins

Content Provider	Springer Nature Link
Author	Parker, Michael S. Parker, Steven L.
Copyright Year	2009
Abstract	The minimal size of the fourth intracellular domain of heptahelical G-protein coupling receptors (GPCRs) is close to 15 residues, and a juxtamembrane 15-residue segment is predicted as helical (Helix-8) in most of the receptors. Sequences of opsins, non-visual opsin-like (family A) GPCRs and Taste-2 receptors correspond with bovine rhodopsin at four positions in this tract. This is especially evident in monoamine receptors. In most GPCRs, the conserved juxtamembrane segment also has a large fraction of basic sidechains, and a considerable excess of cationic over anionic residues. The conservation is not dependent on the preferred G-protein α subunit or the overall length of the domain, indicating an additive speciation. In rod opsins and some A-GPCRs this segment has been shown to associate with the bilayer and to interact with G-proteins. The segment could also be involved in precoupling of receptors and transducers. These interactions could be helped by both the structural propensities and the high content of cationic sidechains.
Starting Page	1
Ending Page	13
Page Count	13
File Format	PDF
ISSN	09394451
Journal	Amino Acids
Volume Number	38
Issue Number	1
e-ISSN	14382199
Language	English
Publisher	Springer Vienna
Publisher Date	2009-06-30
Publisher Place	Vienna
Access Restriction	Subscribed
Subject Keyword	Basic sidechain abundance Cytoplasmic helix Juxtamembrane conservation Receptor phylogeny Transducer activation Transducer recognition Neurobiology Proteomics Life Sciences Biochemical Engineering Analytical Chemistry Biochemistry
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Biochemistry Clinical Biochemistry

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