[HTML][HTML] Helix 8 of the leukotriene B4 receptor is required for the conformational change to the low affinity state after G-protein activation
Recent studies have revealed that G-protein-coupled receptors contain a putative
cytoplasmic helical domain, helix 8. Leukotriene B 4 (LTB 4) receptor 1 derivatives with
truncated or mutated helix 8 showed much higher LTB 4 binding than wild-type (WT)
receptors. Similar to the WT receptor, LTB 4 promoted guanosine 5′-3-O-(thio) triphosphate
(GTPγS) binding in these mutants. Unlike the WT receptor, however, the addition of GTPγS
did not inhibit LTB 4 binding to the mutant receptors. Scatchard analyses revealed that …
cytoplasmic helical domain, helix 8. Leukotriene B 4 (LTB 4) receptor 1 derivatives with
truncated or mutated helix 8 showed much higher LTB 4 binding than wild-type (WT)
receptors. Similar to the WT receptor, LTB 4 promoted guanosine 5′-3-O-(thio) triphosphate
(GTPγS) binding in these mutants. Unlike the WT receptor, however, the addition of GTPγS
did not inhibit LTB 4 binding to the mutant receptors. Scatchard analyses revealed that …