Importance of the extracellular loops in G protein-coupled receptors for ligand recognition and receptor activation.
By M. C. Peeters, G. V. van Westen, Q. Li, Adriaan P. IJzerman. 2011
229 citations recorded by the source corpus.
Subfields: Cellular and Molecular Neuroscience, Molecular Biology
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In Cellular and Molecular Neuroscience
In Molecular Biology
Citations in the corpus
- Improving homology modeling from low-sequence identity templates in Rosetta: A case study in GPCRs (2020, background): “However, despite sequence divergence, there is evidence for structural conservation in these regions [36].”
- Loss of constitutive activity is correlated with increased thermostability of the human adenosine A2A receptor (2013, background): “…ofPharmacology DOI:10.1111/bph.12165 www.brjpharmacol.org 988 British Journal of Pharmacology (2013) 169 988–998 © 2013 The Authors British Journal of Pharmacology © 2013 The British Pharmacological Society requirement for recognition and binding of a wide range of ligands (Peeters et al., 2011).”
- Lifting the lid on GPCRs: the role of extracellular loops (2011, background): “…(CAMs) of the thyroid stimulating hormone receptor have been reported for all three ECLs (Duprez et al., 1998), and agonist-mediated receptor activation of GPCRs can include an essential role for residues in ECL1 (Hawtin et al., 2006; Peeters et al., 2011b) and ECL3 (Lawson and Wheatley, 2004).”
- Structure of the human histamine H1 receptor complex with doxepin (2011, unknown): “Moreover, because of its deep binding position, doxepin does not interact with ECL2, whose highly variable primary and tertiary structures are known to contribute to binding specificity of GPCR ligand”