Structure of CC chemokine receptor 2 with orthosteric and allosteric antagonists

Allosteric nanobodies reveal the dynamic range and diverse mechanisms of G-protein-coupled receptor activation

(2016) Dean P. Staus et al.   NATURE

Structural Insights into the Dynamic Process of β 2 -Adrenergic Receptor Signaling

(2015) Aashish Manglik et al.   CELL

Structures of G protein-coupled receptors reveal new opportunities for drug discovery

(2015) Robert M. Cooke et al.   DRUG DISCOVERY TODAY

“Chemokine receptors as therapeutic targets: Why aren’t there more drugs?”

(2015) Roberto Solari et al.   EUROPEAN JOURNAL OF PHARMACOLOGY

Structural basis for chemokine recognition and activation of a viral G protein-coupled receptor

(2015) J. S. Burg et al.   SCIENCE

Crystal structure of the chemokine receptor CXCR4 in complex with a viral chemokine

(2015) L. Qin et al.   SCIENCE

The High-Resolution Structure of Activated Opsin Reveals a Conserved Solvent Network in the Transmembrane Region Essential for Activation

(2015) Elise Blankenship et al.   STRUCTURE

Discovery of a Potent and Orally Bioavailable Dual Antagonist of CC Chemokine Receptors 2 and 5

(2015) Percy H. Carter et al.   ACS Medicinal Chemistry Letters

CCL2-CCR2 Signaling in Disease Pathogenesis

(2015) Tracy O’Connor et al.   Endocrine Metabolic & Immune Disorders-Drug Targets

Structure of the human P2Y12 receptor in complex with an antithrombotic drug

(2014) Kaihua Zhang et al.   NATURE

Structure of the CCR5 Chemokine Receptor-HIV Entry Inhibitor Maraviroc Complex

(2013) Q. Tan et al.   SCIENCE

Structure-Function of the G Protein–Coupled Receptor Superfamily

(2012) Vsevolod Katritch et al.   Annual Review of Pharmacology and Toxicology

Chemokine Receptor Antagonists

(2012) James Pease et al.   JOURNAL OF MEDICINAL CHEMISTRY

Overview of theCCP4 suite and current developments

(2011) Martyn D. Winn et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Pharmacological modulation of chemokine receptor function

(2011) DJ Scholten et al.   BRITISH JOURNAL OF PHARMACOLOGY

Crystal structure of the β2 adrenergic receptor–Gs protein complex

(2011) Søren G. F. Rasmussen et al.   NATURE

XDS

(2010) Wolfgang Kabsch   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Features and development ofCoot

(2010) P. Emsley et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

PHENIX: a comprehensive Python-based system for macromolecular structure solution

(2010) Paul D. Adams et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Structures of the CXCR4 Chemokine GPCR with Small-Molecule and Cyclic Peptide Antagonists

(2010) B. Wu et al.   SCIENCE

MolProbity: all-atom structure validation for macromolecular crystallography

(2009) Vincent B. Chen et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Rastering strategy for screening and centring of microcrystal samples of human membrane proteins with a sub-10  m size X-ray synchrotron beam

(2009) V. Cherezov et al.   Journal of the Royal Society Interface

Elucidation of Binding Sites of Dual Antagonists in the Human Chemokine Receptors CCR2 and CCR5

(2009) S. E. Hall et al.   MOLECULAR PHARMACOLOGY

Crystallizing membrane proteins using lipidic mesophases

(2009) Martin Caffrey et al.   Nature Protocols

Synthesis and evaluation of cis-3,4-disubstituted piperidines as potent CC chemokine receptor 2 (CCR2) antagonists

(2008) Robert J. Cherney et al.   BIOORGANIC & MEDICINAL CHEMISTRY LETTERS

Discovery of Potent, Orally Bioavailable Small-Molecule Inhibitors of the Human CCR2 Receptor

(2008) Julien Doyon et al.   ChemMedChem

Discovery of Disubstituted Cyclohexanes as a New Class of CC Chemokine Receptor 2 Antagonists

(2008) Robert J. Cherney et al.   JOURNAL OF MEDICINAL CHEMISTRY

Identification of a Putative Intracellular Allosteric Antagonist Binding-Site in the CXC Chemokine Receptors 1 and 2

(2008) D. J. Nicholls et al.   MOLECULAR PHARMACOLOGY

Microscale Fluorescent Thermal Stability Assay for Membrane Proteins

(2008) Alexander I. Alexandrov et al.   STRUCTURE