B. Kobilka

Publications540
h-index128
Citations63,696
Highly Influential Citations2,349
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Crystal Structure of the β2Adrenergic Receptor-Gs protein complex
TLDR
This crystal structure represents the first high-resolution view of transmembrane signalling by a GPCR and the most surprising observation is a major displacement of the α-helical domain of Gαs relative to the Ras-like GTPase domain.
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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 μ-opioid receptor bound to a morphinan antagonist
TLDR
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.
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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 of the human M2 muscarinic acetylcholine receptor bound to an antagonist
TLDR
The structure of the antagonist-bound human M2 receptor is reported, the first human acetylcholine receptor to be characterized structurally, to the authors' knowledge, and provides insights into the challenges of developing subtype-selective ligands for muscarinic receptors and their propensity for allosteric regulation.
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ERK Plays a Regulatory Role in Induction of LTP by Theta Frequency Stimulation and Its Modulation by β-Adrenergic Receptors
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