2018•Worldwide Protein Data BankOpen access

Structure of beta2 adrenergic receptor bound to BI167107, Nanobody 6B9, and a positive allosteric modulator

Xiangyu Liu, Ali Masoudi, Alem W. Kahsai, Li-Yin Huang, Biswaranjan Pani, K. Hirata, S. Ahn, R.J. Lefkowitz, B.K. Kobilka

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Abstract

-adrenergic receptor. Diversity in location, mechanism, and selectivity of allosteric ligands provides potential to expand the range of receptor drugs.

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-adrenergic receptor. Diversity in location, mechanism, and selectivity of allosteric ligands provides potential to expand the range of receptor drugs.

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OpenAlex reports 79 citations for this work. Citation counts describe recorded attention and do not establish research quality.

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Available abstract

-adrenergic receptor. Diversity in location, mechanism, and selectivity of allosteric ligands provides potential to expand the range of receptor drugs.

Key concepts: Allosteric regulation, Allosteric modulator, Receptor, Agonist, Functional selectivity, Chemistry, Intracellular, G protein-coupled receptor

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Structure of beta2 adrenergic receptor bound to BI167107, Nanobody 6B9, and a positive allosteric modulator — Research Paper | ScholarLens