Hendus-Altenburger et al. provide biochemical, structural and functional information on the lipid interaction domain (LID) of the Na+/H+ Exchanger 1 (NHE1). They find that NHE1-LID is intrinsically disordered, but, when allowed to interact with a lipid membrane, forms a helical αα-hairpin, stabilized by hydrophobic and electrostatic interactions. This co-structure is fundamental for NHE1 activity, giving insight into membrane protein regulation via disordered domains.
- Ruth Hendus-Altenburger
- Jens Vogensen
- Birthe B. Kragelund
