Employing information theoretic measures and mutagenesis to identify residues critical for drug-proton antiport function in Mdr1p of Candida albicans.

ABSTRACT: By employing information theoretic measures, this study presents a structure and functional analysis of a multidrug-proton antiporter Mdr1p of Candida albicans. Since CaMdr1p belongs to drug-proton antiporter (DHA1) family of Major Facilitator Superfamily (MFS) of transporters, we contrasted DHA1 (antiporters) with Sugar Porter family (symporters). Cumulative Relative Entropy (CRE) calculated for these two sets of alignments enabled us to selectively identify conserved residues of not only CaMdr1p but for the entire DHA1 family. Based on CRE, the highest scoring thirty positions were selected and predicted to impart functional specificity to CaMdr1p as well as to other drug-proton antiporters. Nineteen positions wherein the CaMdr1p residue matched with the most frequent amino acid at a par

SUBMITTER: Kapoor K 

PROVIDER: S-EPMC2883579 | biostudies-literature | 2010 Jun

REPOSITORIES: biostudies-literature