What is it about?
This work provides the first systematic mutational structure-function analysis of a highly conserved amino acid sequence motif of the major facilitator superfamily. We predicted that the alpha-helix formed by the antiporter motif (motif C) is kinked.
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Why is it important?
The alpha-helix structure formed by the antiporter motif is widely conserved, from bacteria to humans, and appears to play key functional roles in antimicrobial transporters, including multidrug efflux pumps. The antiporter motif structure may form the basis of novel targets for modulation of multidrug resistance.
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This page is a summary of: Mutational analysis and molecular modelling of an amino acid sequence motif conserved in antiporters but not symporters in a transporter superfamily, Molecular Membrane Biology, January 1995, Taylor & Francis, DOI: 10.3109/09687689509072433.
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