Fatty acid induced remodeling within the human liver fatty acid-binding protein

J Biol Chem. 2011 Sep 9;286(36):31924-8. doi: 10.1074/jbc.M111.270165. Epub 2011 Jul 8.

Abstract

We crystallized human liver fatty acid-binding protein (LFABP) in apo, holo, and intermediate states of palmitic acid engagement. Structural snapshots of fatty acid recognition, entry, and docking within LFABP support a heads-in mechanism for ligand entry. Apo-LFABP undergoes structural remodeling, where the first palmitate ingress creates the atomic environment for placement of the second palmitate. These new mechanistic insights will facilitate development of pharmacological agents against LFABP.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Apoproteins
  • Crystallization
  • Crystallography, X-Ray
  • Fatty Acid-Binding Proteins / chemistry*
  • Fatty Acid-Binding Proteins / metabolism
  • Fatty Acids / metabolism*
  • Humans
  • Models, Chemical*
  • Palmitates / chemistry*
  • Protein Binding

Substances

  • Apoproteins
  • Fatty Acid-Binding Proteins
  • Fatty Acids
  • Palmitates

Associated data

  • PDB/3STK
  • PDB/3STM
  • PDB/3STN