1G5W

SOLUTION STRUCTURE OF HUMAN HEART-TYPE FATTY ACID BINDING PROTEIN

Summary for 1G5W

• Entry DOI: 10.2210/pdb1g5w/pdb
• Related: 1BWY 1HMR 1HMS 1HMT 2HMB
• Descriptor: FATTY ACID-BINDING PROTEIN (1 entity in total)
• Functional Keywords: nmr spectroscopy, protein-ligand interactions, selected-fit binding, lipid binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P05413
• Total number of polymer chains: 1
• Total formula weight: 14747.83

Authors

Luecke, C.,Rademacher, M.,Zimmerman, A.,van Moerkerk, H.T.B.,Veerkamp, J.H.,Rueterjans, H. (deposition date: 2000-11-02, release date: 2001-03-07, Last modification date: 2024-05-22)

Primary citation

Lucke, C.,Rademacher, M.,Zimmerman, A.W.,van Moerkerk, H.T.,Veerkamp, J.H.,Ruterjans, H.
Spin-system heterogeneities indicate a selected-fit mechanism in fatty acid binding to heart-type fatty acid-binding protein (H-FABP).
Biochem.J., 354:259-266, 2001

PubMed Abstract: Recent advances in the characterization of fatty acid-binding proteins (FABPs) by NMR have enabled various research groups to investigate the function of these proteins in aqueous solution. The binding of fatty acid molecules to FABPs, which proceeds through a portal region on the protein surface, is of particular interest. In the present study we have determined the three-dimensional solution structure of human heart-type FABP by multi-dimensional heteronuclear NMR spectroscopy. Subsequently, in combination with data collected on a F57S mutant we have been able to show that different fatty acids induce distinct conformational states of the protein backbone in this portal region, depending on the chain length of the fatty acid ligand. This indicates that during the binding process the protein accommodates the ligand molecule by a "selected-fit" mechanism. In fact, this behaviour appears to be especially pronounced in the heart-type FABP, possibly due to a more rigid backbone structure compared with other FABPs, as suggested by recent NMR relaxation studies. Thus differences in the dynamic behaviours of these proteins may be the key to understanding the variations in ligand affinity and specificity within the FABP family.

PubMed: 11171102
DOI: 10.1042/0264-6021:3540259

Experimental method

SOLUTION NMR