By Tobias Langenhan, Torsten Schöneberg
Latest examine on Adhesion GPCRs has unearthed astonishing revelations in regards to the occasions that govern the sign transduction of those receptor molecules and the mobile and organ requisites for those signs. unforeseen and unparalleled findings recommend that Adhesion GPCRs represent a gaggle of receptors that experience mechanical stimuli and transcode them into metabotropic signs during the motion of a unique activation paradigm. Interdisciplinary efforts transcending many parts of biomedical learn together with pharmacology, body structure, genetics, mobile biology, structural biology, biochemistry and bioinformatics have been essential to unveil those primary homes. The medical leaders within the box that carried this study attempt have teamed up right here to supply a finished review of our present figuring out, how Adhesion GPCRs sign and the way those receptors form organ constitution and function.
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Additional info for Adhesion G Protein-coupled Receptors: Molecular, Physiological and Pharmacological Principles in Health and Disease
Mol Pharmacol 82(5):777–783. 080309, PubMed PMID: 22821233, PubMed Central PMCID: PMC3477231 36 A. Krishnan et al. 49. Underwood CR, Garibay P, Knudsen LB, Hastrup S, Peters GH, Rudolph R et al (2010) Crystal structure of glucagon-like peptide-1 in complex with the extracellular domain of the glucagon-like peptide-1 receptor. J Biol Chem 285(1):723–730. M109. 033829, PubMed PMID: 19861722, PubMed Central PMCID: PMC2804221 50. Wouters MA, Rigoutsos I, Chu CK, Feng LL, Sparrow DB, Dunwoodie SL (2005) Evolution of distinct EGF domains with specific functions.
ADGRCs are among the oldest aGPCRs. ADGRC consists of nine cadherin repeats (110 aa), followed by six EGF-like domains (see Sect. 1), two LAG domains, and an HBD (see Sect. 1). The cadherin repeats play a role in extracellular calcium binding . The 3D structure of several cadherin domains in other proteins has been solved lately. These cadherin domains are formed by seven beta-strands and show similarity to immunoglobulin constant domains [91, 92]. Comparable with EGF-like repeats, the quaternary structural composition of several repeats is mediated by calcium binding .
Arac¸ D, Stra¨ter N, Seiradake E (2016) Understanding the structural basis of adhesion GPCR functions. In: Langenhan T, Sch€ oneberg T (eds) Adhesion G protein-coupled receptors: molecular, physiological and pharmacological principles in health and disease. Springer, Heidelberg 43. Lin HH, Stacey M, Yona S, Chang GW (2010) GPS proteolytic cleavage of adhesion-GPCRs. Adv Exp Med Biol 706:49–58, PMID: 21618825 44. Promel S, Langenhan T, Arac D (2013) Matching structure with function: the GAIN domain of adhesion-GPCR and PKD1-like proteins.