D. Rosenbaum

Publications144
h-index43
Citations15,940
Highly Influential Citations693
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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.
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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.
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Structure of a nanobody-stabilized active state of the β2 adrenoceptor
TLDR
A camelid antibody fragment to the human β2 adrenergic receptor is generated, and an agonist-bound, active-state crystal structure of the receptor-nanobody complex is obtained, providing insights into the process of agonist binding and activation.
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Crystal structure of the human beta2 adrenergic G-protein-coupled receptor.
TLDR
The human beta2 adrenoceptor (beta2AR), which was crystallized in a lipid environment when bound to an inverse agonist and in complex with a Fab that binds to the third intracellular loop, differs from rhodopsin in having weaker interactions between the cytoplasmic ends of transmembrane (TM)3 and TM6, involving the conserved E/DRY sequences.
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The structure and function of G-protein-coupled receptors
G-protein-coupled receptors (GPCRs) mediate most of our physiological responses to hormones, neurotransmitters and environmental stimulants, and so have great potential as therapeutic targets for a…
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GPCR Engineering Yields High-Resolution Structural Insights into β2-Adrenergic Receptor Function
TLDR
Analysis of adrenergic receptor ligand-binding mutants within the context of the reported high-resolution structure of β2AR-T4L provides insights into inverse-agonist binding and the structural changes required to accommodate catecholamine agonists.
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Structure and Dynamics of the M3 Muscarinic Acetylcholine Receptor
TLDR
The structure of the Gq/11-coupled M3 mAChR (‘M3 receptor’, from rat) bound to the bronchodilator drug tiotropium is described and a structural comparison between two members of a mammalian GPCR subfamily displaying different G-protein coupling selectivities is allowed.
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Crystal structure of the human β2 adrenergic G-protein-coupled receptor
TLDR
The β2AR structure differs from rhodopsin in having weaker interactions between the cytoplasmic ends of transmembrane (TM)3 and TM6, involving the conserved E/DRY sequences, which may be responsible for the relatively high basal activity and structural instability of the β2 AR.
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Structure and Function of an Irreversible Agonist-β2 Adrenoceptor complex
TLDR
A covalent agonist-bound β2AR–T4L fusion protein is designed that can be covalently tethered to a specific site on the receptor through a disulphide bond, and is capable of activating a heterotrimeric G protein.
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Ligand-specific regulation of the extracellular surface of a G protein coupled receptor
TLDR
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.
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