Native cysteines and cysteine substitutions in the transmembrane domain of ASIC1a.
Miguel Xavier van Bemmelen
Delphine Huser
Ivan Gautschi
Laurent Schild
10.1371/journal.pone.0135191.g002
https://plos.figshare.com/articles/figure/_Native_cysteines_and_cysteine_substitutions_in_the_transmembrane_domain_of_ASIC1a_/1506172
<p>A: Model structure of a human ASIC1a subunit based on the chicken ASIC1 crystal structure as published elsewhere [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0135191#pone.0135191.ref004" target="_blank">4</a>]: the subunit is made of 2 transmembrane α helices (TM1 and TM2); the cysteines C49, C59 and C61 in the transmembrane α helix 1 (TM1) are shown in green. The substituted cysteines G430C and G433C are in the TM2, and V74C and Y426C are located at the entrance of the channel pore in the extracellular vestibule (ECV). B: Top view of the transmembrane α helices TM1 and TM2 of a single ASIC1a subunit, with the pore lining residues G433C and G430C according to Li et al. 2011. C: Representative recordings of ASIC1a currents elicited at pH 5.5 in the absence (black) or in the presence (red) of 100 μM Cd<sup>2+</sup> in xenopus oocytes expressing either ASIC1a wt or the V74C, Y426C, G430C, G433C mutants.</p>
2015-08-07 04:03:38
extracellular pore vestibule
oligomeric states
ASIC 1a complexes
Xenopus laevis oocytes
sulfhydryl crosslinker BMOE
Homotetrameric Assembly State
ASIC 1a monomers
crosslinking conditions ASIC 1a
ASIC 1a oligomers
ASIC 1a subunit
cell surface
ASIC 1a channel
tetrameric concatemeric cDNA
cho
ASIC 1a homotetramer
ASIC 1 complexes