2007
DOI: 10.1074/jbc.m607492200
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Tryptophan-scanning Mutagenesis in the αM3 Transmembrane Domain of the Muscle-type Acetylcholine Receptor

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Cited by 21 publications
(45 citation statements)
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“…Thus, the AChR serves as an excellent model to test the validity of the FT-TrpScanM approach and provides reassurance on its capacity to generate trustworthy predictions of the secondary structures of membrane protein LETMDs in general. Furthermore, FT-TrpScanM supports and validates the conclusion from previous TrpScanM [1][2][3][4][5] and biochemical [28][29][30] studies, which predicted that the LETMDs are arranged as α-helical structures. In addition, using this approach, we were able to provide additional structural information, estimate mean periodicities, determine the minimum number of consecutive tryptophan substitutions required to reliably predict α-helical structures, and assess the quality of structure predictions.…”
Section: Introductionsupporting
confidence: 85%
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“…Thus, the AChR serves as an excellent model to test the validity of the FT-TrpScanM approach and provides reassurance on its capacity to generate trustworthy predictions of the secondary structures of membrane protein LETMDs in general. Furthermore, FT-TrpScanM supports and validates the conclusion from previous TrpScanM [1][2][3][4][5] and biochemical [28][29][30] studies, which predicted that the LETMDs are arranged as α-helical structures. In addition, using this approach, we were able to provide additional structural information, estimate mean periodicities, determine the minimum number of consecutive tryptophan substitutions required to reliably predict α-helical structures, and assess the quality of structure predictions.…”
Section: Introductionsupporting
confidence: 85%
“…It is noteworthy that we took advantage of the recently reported structure of the Torpedo AChR, which was determined at 4 Å resolution using cryo-electron microscopy in order to corroborate our predictions [26]. Interestingly, the TrpScanM predicted α-helical structures for the LETMDs [1][2][3][4][5] even when a lower-resolution cryoelectron microscopy structure mistakenly predicted the LETMDs to be arranged as β-sheets [27]. Thus, the AChR serves as an excellent model to test the validity of the FT-TrpScanM approach and provides reassurance on its capacity to generate trustworthy predictions of the secondary structures of membrane protein LETMDs in general.…”
Section: Introductionsupporting
confidence: 59%
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“…Tryptophan substitution has been employed at GABA A Rs to elucidate transmembrane domain binding sites for alcohols and anesthetics (30,31), at nAChRs to define transmembrane helical structure and dynamics (32,33) and at P 2 X receptors to investigate movements induced by ivermectin (34). Glycine dose-response relationships were quantitated for all these mutant GlyRs to establish whether the substitutions were well tolerated by the receptor.…”
Section: Disruption Of Ivermectin Efficacy Via Mutations At the Lbd-tmdmentioning
confidence: 99%
“…39,[46][47][48] The normalized maximum response corresponds to the maximum current (I max ) divided by the total number of receptors as determined by 125 I-labaled α-BTX binding assays. Therefore, if only a fraction of the total number of receptors contributes to the activatable pool, then I max will be lower than expected, resulting in a decreased normalized maximum response.…”
Section: Discussionmentioning
confidence: 99%