β2AR agonist
BI-167107
BI-167107 is a highly potent and long-acting β2 adrenergic receptor (β2AR) agonist. As a result, BI-167107 was used to support the crystallization of the active state of the β2AR and β2AR-G-protein complexes. It is not a selective β2-agonist, so its only recommended use is as a tool to support crystallization studies of other beta receptors1-5, such as β1AR.
More information
G-protein-coupled receptors (GPCRs) are integral membrane proteins that have an essential role in human physiology, yet only recently we started to understand the molecular processes through which they bind to their endogenous agonists and activate effector proteins. β2AR is a member of the class A family of GPCRs. Besides rhodopsin it is the best characterized member of that family.
β2 adrenergic receptor (β2AR) agonists have been used as bronchodilating agent for the last decades for the treatment of pulmonary diseases like asthma. BI-167107 was synthesized during a campaign to develop third generation of β2-agonists. Interestingly BI-167107 is also very active agonist of the β1AR (IC50 = 3.2 nM) and shows some activity as α1A antagonist (IC50 = 32 nM).
Human β2AR in the active state, in complex with BI-167107 (PDB code: 3p0g).
We recommend using this compound only to support the crystallization of beta receptors.
BI-167107 is a potent and long-acting beta agonist with a KD of 84 pM.
PROBE NAME | BI-167107 |
| MW [Da, free base]a | 370.4 |
| β2AR KD [nM]b | 0.084 |
| β2AR Bmax [nM]b | 2238 |
| EC50 cAMP accumulation [nM]b | 0.05 |
| t1/2 (dissociation half-life) [h]b | 30 |
aFor the salt form you will get, please refer to the label on the vial and for the molecular weight of the salt, please refer to the FAQs
bFor further information on assays please refer to reference 1.
BI-167107 is not a selective β2 agonist.
A Eurofins Safety Panel 44™ screen revealed several hits >70% inhibition at 10µM and IC50s were consequently measured for eight targets. Two showed strong activity in the low nanomolar range: β1(h) (agonist radioligand) (IC50 = 3.2 nM), α1A(h) (antagonist radioligand) (IC50 = 32 nM). BI-167107 showed weaker activity on the other targets: 5-HT transporter (h) (antagonist radioligand) (IC50 = 6.1 µM ), 5-HT1A(h) (agonist radioligand) (IC50 = 1.4 µM), 5-HT1B (antagonist radioligand) (IC50 = 0.25 µM), D2S(h) (agonist radioligand) (IC50 = 5.9 µM), dopamine transporter(h) (antagonist radioligand) (IC50 = 7.2 µM), μ (MOP) (h) (agonist radioligand) (IC50 = 6.5 µM).
The data is available for download.
| SELECTIVITY DATA AVILABLE | BI-167107 |
SafetyScreen44™ with kind support of  | Yes |
| Invitrogen® | No |
| DiscoverX® | No |
| Dundee | No |
Download selectivity data:
BI-167107_selectivityData_0.xlsx
PDB ID | TITLE |
| 3P0G | Structure of a nanobody-stabilized active state of the β2AR |
| 4LDE | Structure of β2AR bound to BI-167107 and an engineered nanobody |
| 3SN6 | Crystal structure of the β2AR-Gs protein complex |
BI-167107 was used to support crystallization of active state β2AR complexes and can be employed as a tool for the crystallization of other beta receptors.
2D structure formats available
Structure of a nanobody-stabilized active state of the β2 adrenoceptor
Rasmussen S. G. F., Choi H.-J., Fung J. J., Pardon E., Casarosa P., Chae P. S., DeVree B. T., Rosenbaum D. B., Thian F. S, Kobilka T. S., Schnapp A, Konetzki I., Sunahara R. K., Gellman S. H., Pautsch A., Steyaert J., Weis W. I., Kobilka B. K.
Nature 2011, 469, 175-180
Crystal structure of the β2 adrenergic receptor-Gs protein complex
Rasmussen S. G. F., DeVree B. T., Zou Y., Kruse A. C., Chung K. Y., Kobilka T. S., Thian F. S., Chae P. S., Pardon E., Calinski D., Mathiesen J. M., Shah S. T. A., Lyons J. A., Caffrey M., Gellman S. H., Steyaert J., Skiniotis G., Weis W. I., Sunahara R. K., Kobilka B. K.
Nature 2011, 477, 549-555
When you plan a publication, please use the following acknowledgement:
BI-167107 was kindly provided by Boehringer Ingelheim via its open innovation platform opnMe, available at https://www.opnme.com.