Refined structures of mouse P-glycoprotein.

ABSTRACT: The recently determined C. elegans P-glycoprotein (Pgp) structure revealed significant deviations compared to the original mouse Pgp structure, which suggested possible misinterpretations in the latter model. To address this concern, we generated an experimental electron density map from single-wavelength anomalous dispersion phasing of an original mouse Pgp dataset to 3.8 Å resolution. The map exhibited significantly more detail compared to the original MAD map and revealed several regions of the structure that required de novo model building. The improved drug-free structure was refined to 3.8 Å resolution with a 9.4 and 8.1% decrease in R(work) and R(free), respectively, (R(work)  = 21.2%, R(free) = 26.6%) and a significant improvement in protein geometry. The improved mouse Pgp model c

SUBMITTER: Li J 

PROVIDER: S-EPMC3892297 | biostudies-literature | 2014 Jan

REPOSITORIES: biostudies-literature