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What is the molecular structure and function of GABBR in the human brain? 


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The GABAB receptor in the human brain is a heterodimeric complex composed of GABAB1 and GABAB2 subunits, crucial for inhibitory neurotransmission. GABAB1 contains the GABA-binding site, while GABAB2 mediates G protein-coupled signaling. Cryo-EM studies have revealed the receptor's structure, showing ligands preassociated with the receptor and an intersubunit latch maintaining the inactive state. Variants in GABBR1 have been linked to motor delay, epilepsy, and other neurological conditions, affecting receptor activation by GABA. The extracellular loop 2 of GABAB plays a vital role in structural transitions and interacts with phospholipids, influencing signal transduction and potential drug targeting. Understanding the molecular intricacies of GABAB receptors is essential for elucidating their physiological effects and developing therapeutic interventions.

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The GABAB receptor in the human brain functions as an obligate heterodimer, with extracellular loop 2 playing a crucial role in signal transduction by connecting ligand binding to G protein activation.
The GABAB receptor in the human brain consists of GABAB1 and GABAB2 subunits with a unique heterodimer interface, maintaining an inactive state crucial for inhibitory neurotransmission.
GABAB receptors in the human brain consist of GABAB1 and GABAB2 subunits, forming heterodimers that regulate synaptic activity through G protein-coupled signaling and ion channel modulation.
GABBR1 and GABBR2 encode GABAB receptor subunits. GABBR1 monoallelic variants lead to neurodevelopmental delay and epilepsy by affecting GABA activation, potentially altering the excitation/inhibition balance in the brain.
The molecular structure and function of GABAB receptors in the human brain involve modulation of neuronal signals through pre- and postsynaptic actions, impacting neurological diseases and potential drug discovery.

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