Ontology highlight
ABSTRACT:
SUBMITTER: Chen X
PROVIDER: S-EPMC3890798 | biostudies-literature | 2014 Jan
REPOSITORIES: biostudies-literature
Proceedings of the National Academy of Sciences of the United States of America 20131223 1
Three deep-pore locations, L312, A313, and A316, were identified in a scanning mutagenesis study of the BK (Ca(2+)-activated, large-conductance K(+)) channel S6 pore, where single aspartate substitutions led to constitutively open mutant channels (L312D, A313D, and A316D). To understand the mechanisms of the constitutive openness of these mutant channels, we individually mutated these three sites into the other 18 amino acids. We found that charged or polar side-chain substitutions at each of th ...[more]