Figure 1.
Figure 1. Location of the L119 residue in a homology model of α7 (Celie et al., 2004). (A) The overview at left shows an α7-α7 homodimer and the location of the L119 residue in relation to the C-loop in the primary face of the agonist binding site. The image on the right shows the proximity at increased magnification. Images were created in Deep View (Swiss-PdbViewer; Guex and Peitsch, 1997) from the crystal structure model of the ACh binding protein (deposited in the Protein Data Bank under accession no. 1I9B; Brejc et al., 2001). (B) The effect of MTSEA treatment (2 mM for 60 s) on the ACh-evoked responses of oocytes expressing the α7L119C mutation in a cysteine-null (α7C116S) background. In this experiment, peak current responses to 300 µM ACh were reduced 99.4 ± 0.2%, and net charge was reduced by 99.7 ± 0.1% (n = 4). Responses to 3 mM ACh were reduced to a similar extent: 97.9 ± 0.3 and 95.9 ± 2.0% for peak current and net charge, respectively (n = 4).

Location of the L119 residue in a homology model of α7 (Celie et al., 2004). (A) The overview at left shows an α7-α7 homodimer and the location of the L119 residue in relation to the C-loop in the primary face of the agonist binding site. The image on the right shows the proximity at increased magnification. Images were created in Deep View (Swiss-PdbViewer; Guex and Peitsch, 1997) from the crystal structure model of the ACh binding protein (deposited in the Protein Data Bank under accession no. 1I9B; Brejc et al., 2001). (B) The effect of MTSEA treatment (2 mM for 60 s) on the ACh-evoked responses of oocytes expressing the α7L119C mutation in a cysteine-null (α7C116S) background. In this experiment, peak current responses to 300 µM ACh were reduced 99.4 ± 0.2%, and net charge was reduced by 99.7 ± 0.1% (n = 4). Responses to 3 mM ACh were reduced to a similar extent: 97.9 ± 0.3 and 95.9 ± 2.0% for peak current and net charge, respectively (n = 4).

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