Communication between the nucleotide binding domains of P-glycoprotein occurs via conformational changes that involve residue 508

Results suggest that the accessibility of residue 508 of alpha-helical subdomain of nucleotide binding domain 1 in P-glycoprotein alters due to ATP hydrolysis mediated confromational changes, thereby facilitating communication between the P-glycoprotein nucleotide binding domains as determined by cysteine-scanning mutagenesis.