Conserved 2nd Residue of Helix 8 of GPCR May Confer the Subclass-Characteristic and Distinct Roles through a Rapid Initial Interaction with Specific G Proteins

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Bibliographische Detailangaben
Zeitschriftentitel:	International Journal of Molecular Sciences
Personen und Körperschaften:	Sato
In:	International Journal of Molecular Sciences, 20, 2019, 7, S. 1752
Format:	E-Article
Sprache:	Englisch
veröffentlicht:	MDPI AG
Schlagwörter:	Inorganic Chemistry Organic Chemistry Physical and Theoretical Chemistry Computer Science Applications Spectroscopy Molecular Biology General Medicine Catalysis

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Zusammenfassung:	<jats:p>To obtain a systematic view of the helix-8-second residue responsible for G protein-coupled receptor (GPCR)–G protein initial specific interactions, 786 human GPCRs were subclassified based on the pairs of agonist groups and target G proteins and compared with their conserved second residue of helix 8. Of 314 non-olfactory and deorphanized GPCRs, 273 (87%) conserved single amino acids in the subclasses, while 93 (58%) of the 160 subclasses possessed only a single GPCR member. Class B, C, Frizzled, and trace amine-associated GPCRs demonstrated 100% conservation, whereas class Ⅰ and Ⅱ olfactory and vomeronasal 1 receptors demonstrated much lower rates of conservation (20–47%). These conserved residues are characteristic of GPCR classes and G protein subtypes and confer their functionally-distinct roles.</jats:p>
Umfang:	1752
ISSN:	1422-0067
DOI:	10.3390/ijms20071752