Intestinal fatty acid-binding protein: the structure and stability of a helix-less variant.

@article{Kim1996IntestinalFA,
  title={Intestinal fatty acid-binding protein: the structure and stability of a helix-less variant.},
  author={Kyoungtae Kim and David P Cistola and Carl Frieden},
  journal={Biochemistry},
  year={1996},
  volume={35 23},
  pages={7553-8}
}
The structure of Escherichia coli-derived rat intestinal fatty acid-binding protein (I-FABP) exhibits a beta-clam topology comprised of two five-stranded antiparallel beta-sheets surrounding a large solvent-filled cavity into which the ligand binds. It also contains two alpha-helices that span residues E15-A32 and join beta-strands A and B. This helical domain is conserved in all proteins of this family for which structures have been determined. In order to assess the structural and functional… CONTINUE READING

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