3p6c: Difference between revisions
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/FABP4_HUMAN FABP4_HUMAN]] Lipid transport protein in adipocytes. Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus (By similarity). | [[http://www.uniprot.org/uniprot/FABP4_HUMAN FABP4_HUMAN]] Lipid transport protein in adipocytes. Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus (By similarity). | ||
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== Publication Abstract from PubMed == | |||
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. | |||
Structural analysis of ibuprofen binding to human adipocyte fatty-acid binding protein (FABP4).,Gonzalez JM, Fisher SZ Acta Crystallogr F Struct Biol Commun. 2015 Feb;71(Pt 2):163-70. doi:, 10.1107/S2053230X14027897. Epub 2015 Jan 28. PMID:25664790<ref>PMID:25664790</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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==See Also== | ==See Also== | ||
*[[Fatty acid-binding protein|Fatty acid-binding protein]] | *[[Fatty acid-binding protein|Fatty acid-binding protein]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 11:13, 25 February 2015
Human adipocyte lipid-binding protein FABP4 in complex with citric acidHuman adipocyte lipid-binding protein FABP4 in complex with citric acid
Structural highlights
Function[FABP4_HUMAN] Lipid transport protein in adipocytes. Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus (By similarity). Publication Abstract from PubMedInhibition 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. Structural analysis of ibuprofen binding to human adipocyte fatty-acid binding protein (FABP4).,Gonzalez JM, Fisher SZ Acta Crystallogr F Struct Biol Commun. 2015 Feb;71(Pt 2):163-70. doi:, 10.1107/S2053230X14027897. Epub 2015 Jan 28. PMID:25664790[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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