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Structures of the CXCR4 Chemokine GPCR with Small-Molecule and Cyclic Peptide Antagonists
TLDR
Five independent crystal structures of CXCR4 bound to an antagonist small molecule IT1t and a cyclic peptide CVX15 at 2.5 to 3.2 angstrom resolution reveal a consistent homodimer with an interface including helices V and VI that may be involved in regulating signaling. Expand
The 2.6 Angstrom Crystal Structure of a Human A2A Adenosine Receptor Bound to an Antagonist
TLDR
The crystal structure of the human A2A adenosine receptor is determined, in complex with a high-affinity subtype-selective antagonist, ZM241385, to 2.6 angstrom resolution and suggests a role for ZM 241385 in restricting the movement of a tryptophan residue important in the activation mechanism of the class A receptors. Expand
High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor.
TLDR
Although the location of carazolol in the beta2-adrenergic receptor is very similar to that of retinal in rhodopsin, structural differences in the ligand-binding site and other regions highlight the challenges in using rhodopin as a template model for this large receptor family. Expand
High-Resolution Crystal Structure of an Engineered Human β2-Adrenergic G Protein–Coupled Receptor
TLDR
Although the location of carazolol in the β2-adrenergic receptor is very similar to that of retinal in rhodopsin, structural differences in the ligand-binding site and other regions highlight the challenges in using rhodopin as a template model for this large receptor family. Expand
Structure of the Human Dopamine D3 Receptor in Complex with a D2/D3 Selective Antagonist
TLDR
The crystal structure of the human dopamine D3 receptor in complex with the small molecule D2R/D3R-specific antagonist eticlopride reveals important features of the ligand binding pocket and extracellular loops. Expand
Structure of an Agonist-Bound Human A2A Adenosine Receptor
TLDR
The molecule UK-432097 is defined as a “conformationally selective agonist” capable of receptor stabilization in a specific active-state configuration and sheds light on G protein–coupled receptor activation. Expand
Structural Basis for Allosteric Regulation of GPCRs by Sodium Ions
TLDR
The high-resolution structure of a stabilized version of the human A2Aadenosine receptor (A2AAR) reveals the position of about 60 internal waters, which suggests an almost continuous channel in the GPCR and can explain the allosteric effects of Na+ on ligand binding and how cholesterol may contribute to G PCR stabilization. Expand
A specific cholesterol binding site is established by the 2.8 A structure of the human beta2-adrenergic receptor.
TLDR
Temperature stability analysis using isothermal denaturation confirms that a cholesterol analog significantly enhances the stability of the receptor, and a consensus motif is defined that predicts cholesterol binding for 44% of human class A receptors, suggesting that specific sterol binding is important to the structure and stability of other G protein-coupled receptors. Expand
Crystal structure of botulinum neurotoxin type A and implications for toxicity
TLDR
The crystal structure of the entire 1,285 amino acid di-chain neurotoxin was determined and the toxin appears as a hybrid of varied structural motifs and suggests a modular assembly of functional subunits to yield pathogenesis. Expand
Structure-function of the G protein-coupled receptor superfamily.
TLDR
High-resolution crystallography of G protein-coupled receptors shows the receptors as allosteric machines that are controlled not only by ligands but also by ions, lipids, cholesterol, and water, and helps redefine knowledge of how GPCRs recognize such a diverse array of ligands. Expand
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