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Extrahelical Binding Site for a 1H-Imidazo[4,5-c]quinolin-4-amine A₃ Adenosine Receptor Positive Allosteric Modulator on Helix 8 and Distal Portions of Transmembrane Domains 1 and 7.

ABSTRACT: This study describes the localization and computational prediction of a binding site for the A₃ adenosine receptor (A₃AR) positive allosteric modulator 2-cyclohexyl-1H-imidazo[4,5-c]quinolin-4-(3,4-dichlorophenyl)amine (LUF6000). The work reveals an extrahelical lipid-facing binding pocket disparate from the orthosteric binding site that encompasses transmembrane domain (TMD) 1, TMD7, and Helix (H) 8, which was predicted by molecular modeling and validated by mutagenesis. According to the model, the nearly planar 1H-imidazo[4,5-c]quinolinamine ring system lies parallel to the transmembrane segments, inserted into an aromatic cage formed by π-π stacking interactions with the side chains of Y284^7.55 in TMD7 and Y293^8.54 in H8 and by π

SUBMITTER: Fisher CL

PROVIDER: S-EPMC10877738 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature

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Dataset Information

Extrahelical Binding Site for a 1H-Imidazo[4,5-c]quinolin-4-amine A₃ Adenosine Receptor Positive Allosteric Modulator on Helix 8 and Distal Portions of Transmembrane Domains 1 and 7.

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Dataset Information

Extrahelical Binding Site for a 1H-Imidazo[4,5-c]quinolin-4-amine A3 Adenosine Receptor Positive Allosteric Modulator on Helix 8 and Distal Portions of Transmembrane Domains 1 and 7.

OmicsDI is part of the ELIXIR infrastructure

Tweets

Extrahelical Binding Site for a 1H-Imidazo[4,5-c]quinolin-4-amine A₃ Adenosine Receptor Positive Allosteric Modulator on Helix 8 and Distal Portions of Transmembrane Domains 1 and 7.