3RZY

Human adipocyte lipid-binding protein FABP4, Apo form at 1.08 Ang resolution.

Summary for 3RZY

• Entry DOI: 10.2210/pdb3rzy/pdb
• Related: 3p6c 3p6d 3p6e 3p6f 3p6g 3p6h
• Descriptor: Fatty acid-binding protein, adipocyte (2 entities in total)
• Functional Keywords: lipocalin, beta barrel, fatty acid binding protein, lipid binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P15090
• Total number of polymer chains: 1
• Total formula weight: 15485.73

Authors

Gonzalez, J.M.,Pozharski, E. (deposition date: 2011-05-12, release date: 2011-06-29, Last modification date: 2024-02-28)

Primary citation

Gonzalez, J.M.,Fisher, S.Z.
Structural analysis of ibuprofen binding to human adipocyte fatty-acid binding protein (FABP4).
Acta Crystallogr F Struct Biol Commun, 71:163-170, 2015

PubMed Abstract: Inhibition of human adipocyte fatty-acid binding protein (FABP4) has been proposed as a treatment for type 2 diabetes, fatty liver disease and atherosclerosis. However, FABP4 displays a naturally low selectivity towards hydrophobic ligands, leading to the possibility of side effects arising from cross-inhibition of other FABP isoforms. In a search for structural determinants of ligand-binding selectivity, the binding of FABP4 towards a group of small molecules structurally related to the nonsteroidal anti-inflammatory drug ibuprofen was analyzed through X-ray crystallography. Several specific hydrophobic interactions are shown to enhance the binding affinities of these compounds, whereas an aromatic edge-to-face interaction is proposed to determine the conformation of bound ligands, highlighting the importance of aromatic interactions in hydrophobic environments.

PubMed: 25664790
DOI: 10.1107/S2053230X14027897

Experimental method

X-RAY DIFFRACTION (1.08 Å)