Structural insights into a StART-like domain in Lam4 and its interaction with sterol ligands

Biochem Biophys Res Commun. 2018 Jan 15;495(3):2270-2274. doi: 10.1016/j.bbrc.2017.12.109. Epub 2017 Dec 20.

Abstract

Sterols are essential components of cellular membranes and shape their biophysical properties. The recently discovered family of Lipid transfer proteins Anchored at Membrane contact sites (LAMs) has been suggested to carry out intracellular sterol traffic using StART-like domains. Here, we studied the second StART-like domain of Lam4p from S. cerevisiae by NMR. We show that NMR data are consistent with the StART-like domain structure, and that several functionally important regions within the domain exhibit significant conformational dynamics. NMR titration experiments confirm sterol binding to the canonical sterol-binding site and suggest a role of membrane interactions on the thermodynamics and kinetics of sterol binding.

Keywords: Intracellular sterol traffic; Lipid transfer proteins; Membrane contact sites; Nuclear magnetic resonance; Protein-lipid interaction.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Carrier Proteins / chemistry*
  • Carrier Proteins / ultrastructure*
  • Ligands
  • Models, Chemical*
  • Molecular Docking Simulation*
  • Protein Binding
  • Protein Conformation
  • Protein Domains
  • Sterols / chemistry*
  • Structure-Activity Relationship

Substances

  • Carrier Proteins
  • Ligands
  • Sterols
  • lipid transfer protein