Liver fatty acid binding protein: Species variation and the accommodation of different ligands

James Thompson, Amy Reese-Wagoner, Leonard Banaszak

Research output: Contribution to journalReview articlepeer-review

49 Scopus citations


The crystal structure of rat liver fatty acid binding protein (LFABP) and an alignment of amino acid sequences of all known species have been used to demonstrate two groups or sub-classes. Based on estimates at neutral pH and the electrostatic field calculated using the crystal coordinates, some evidence of changes that occur in going from holo- to apo-forms has been obtained. LFABP belongs to a large family frequently referred to as the intracellular lipid binding proteins or iLBPs. LFABP, unlike other family members, has two fatty acid binding sites. The two cavity sites have been reviewed and arguments for interactions between the sites are presented. Based on the crystal structure of rat LFABP, differences between the A and B groups have been postulated. Last of all, hypothetical models have been built of complexes of LFABP and heme, and LFABP and oleoyl CoA. In both cases, the stoichiometry is one to one and the models show why this is likely. Copyright (C) 1999 Elsevier Science B.V.

Original languageEnglish (US)
Pages (from-to)117-130
Number of pages14
JournalBiochimica et Biophysica Acta - Molecular and Cell Biology of Lipids
Issue number2-3
StatePublished - Nov 23 1999


  • Beta barrel
  • Fatty acid
  • Fatty acid binding protein
  • Heme
  • Intracellular lipid binding protein

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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