A single lysyl residue defines the binding specificity of a human odorant‐binding protein for aldehydes
Authors:
- Claude NespoulousCNClaude Nespoulous
- Jean-Claude PernolletJPJean-Claude Pernollet
- Loïc BriandLBLoïc Briand
- 15 March 2006
- journal article
- Published by Wiley in FEBS Letters
- Vol. 580 (8) , 2102-2108
Abstract
Odorant‐binding proteins (OBPs) are small abundant soluble proteins belonging to the lipocalin superfamily, which are thought to carry hydrophobic odorants through aqueous mucus towards olfactory receptors. Human variant hOBP‐2A has been demonstrated to bind numerous odorants of different chemical classes with a higher affinity for aldehydes and fatty acids. Three lysyl residues of the binding pocket (Lys62, Lys82 and Lys112) have been suggested as candidates for playing such a role. Here, using site‐directed mutagenesis and fluorescent probe displacements, we show that Lys112 is the major determinant for governing hOBP‐2A specificity towards aldehydes and small carboxylic acids.Keywords
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