Characterization of crystalline rat liver fatty acid binding protein produced in Escherichia coli

N. S. Winter, J. I. Gordon, J. Banaszak

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

The principal absorptive cell of the rat small intestinal epithelium contains two homologous cytosolic proteins that bind long chain fatty acids. These are known as intestinal and liver fatty acid binding proteins (FABP). While their precise physiological roles have not been defined, they are believed to represent a multifunctional cytosolic transport system that is involved in the trafficking of exogenous lipids to sites of metabolic processing. 13C NMR studies have revealed differences in their fatty acid binding stoichiometries, binding mechanisms, and the ionization properties of bound fatty acids. To understand the functional differences, liver FABP has been crystallized for eventual comparison with the known crystal structure of intestinal FABP. The lattice type is trigonal with unit cell dimensions of a = b = 84.1 Å and c = 44.2 Å+. The space group as determined by examination of the Patterson symmetry is either P3121 or P3221.

Original languageEnglish
Pages (from-to)10955-10958
Number of pages4
JournalJournal of Biological Chemistry
Volume265
Issue number19
StatePublished - 1990

Fingerprint

Dive into the research topics of 'Characterization of crystalline rat liver fatty acid binding protein produced in Escherichia coli'. Together they form a unique fingerprint.

Cite this