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Crystal structure of the μ-opioid receptor bound to a morphinan antagonist
The 2.8 Å crystal structure of the mouse µ-OR in complex with an irreversible morphinan antagonist is described, revealing high-resolution insights into opioid receptor structure that will enable the application of structure-based approaches to develop better drugs for the management of pain and addiction.
A molecular dissection of the glycoprotein hormone receptors.
Ligand-specific regulation of the extracellular surface of a G protein coupled receptor
NMR spectroscopy is used to demonstrate conformational coupling between the ECS and the orthosteric binding site, showing that drugs targeting this diverse surface could function as allosteric modulators with high subtype selectivity.
Glycoprotein hormone receptors: determinants in leucine‐rich repeats responsible for ligand specificity
Molecular dynamics simulations and additional site‐directed mutagenesis provided a structural rationale for the evolution of binding specificity in this duplicated gene family.
Pharmacogenomic and structural analysis of constitutive g protein-coupled receptor activity.
A brief historical introduction to the concept of constitutive receptor activity and the pharmacogenomic and structural aspects of constitutively active GPCR activity is provided.
An Activation Switch in the Rhodopsin Family of G Protein-coupled Receptors
This work has identified residue Asn-7.49, of the NPxxY motif of TM 7, as a molecular switch in the mechanism of thyrotropin receptor (TSHr) activation, and focused on the transmembrane region and in particular on a network of polar interactions between highly conserved residues.
Interactions between Intracellular Domains as Key Determinants of the Quaternary Structure and Function of Receptor Heteromers*
Analysis of MAPK signaling in striatal slices of CB1 receptor KO mice and wild-type littermates supported the existence of A1-CB1-D2 receptor heteromer in the brain and allowed the first molecular model of the quaternary structure of a receptor heteromultimer to be proposed.
The Role of Internal Water Molecules in the Structure and Function of the Rhodopsin Family of G Protein‐Coupled Receptors
- L. Pardo, X. Deupí, N. Dölker, M. López-Rodríguez, M. Campillo
- BiologyChembiochem : a European journal of chemical…
- 2 January 2007
The availability of the rhodopsin structure allows the use of homology modeling techniques to build three-dimensional models of other homologous GPCRs, and a large number of conserved sequence patterns suggest a common TM structure.
Activation of CCR5 by Chemokines Involves an Aromatic Cluster between Transmembrane Helices 2 and 3*
- C. Govaerts, A. Bondue, C. Blanpain
- Biology, ChemistryThe Journal of Biological Chemistry
- 17 January 2003
It is suggested that transmembrane helices 2 and 3 of CCR5 contain important structural elements for the activation mechanism of chemokine receptors, and possibly other related receptors as well.
Molecular Basis of Ligand Dissociation in β-Adrenergic Receptors
The steered molecular dynamics simulation method is used to describe, in atomic detail, the unbinding process of two inverse agonists, which have been recently co-crystallized with β1 and β2ARs subtypes, along four different channels and suggests the presence of secondary binding sites located in the extracellular loops 2 and 3 and transmembrane helix 7.