GABA receptor: Difference between revisions

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The GABAB receptor exists in the resting state (Figure 1) and the active state (Figure 2)(Geng, 2013). Using the GABAB crystal structures, Geng et al. found that both subunits exist in open conformations while at rest. Upon binding with the agonist the GABAB1 subunit closes (Geng, 2013) (see below). Additionally, it was found that the agonist is bound to the <scene name='71/716457/Active_site_of_gaba-b/1'>active site</scene>, located at the interdomain crevice of the GABAB1 subunit due to an overlap of amino acid residues (Geng, 2013). This conformation change is highlighted in Figures 1 and 2 in the visible reduction in space between GABAB subunits upon binding with GABA.   
The GABAB receptor exists in the resting state (Figure 1) and the active state (Figure 2)(Geng, 2013). Using the GABAB crystal structures, Geng et al. found that both subunits exist in open conformations while at rest. Upon binding with the agonist the GABAB1 subunit closes (Geng, 2013) (see below). Additionally, it was found that the agonist is bound to the <scene name='71/716457/Active_site_of_gaba-b/1'>active site</scene>, located at the interdomain crevice of the GABAB1 subunit due to an overlap of amino acid residues (Geng, 2013). This conformation change is highlighted in Figures 1 and 2 in the visible reduction in space between GABAB subunits upon binding with GABA.   
 
<scene name='71/716457/Active_site_iwith_gaba_bound/1'>Active site with GABA bound</scene>
== Function ==
== Function ==
<Structure load='4MS3' size='350' frame='true' align='right' caption='Figure 2. Display of the GABAB receptor while in the bound state (Geng, 2013)' scene='Insert optional scene name here' />
<Structure load='4MS3' size='350' frame='true' align='right' caption='Figure 2. Display of the GABAB receptor while in the bound state (Geng, 2013)' scene='Insert optional scene name here' />