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A single lysyl residue defines the binding specificity of a human odorant‐binding protein for aldehydes
Author(s) -
Tcatchoff Lionel,
Nespoulous Claude,
Pernollet Jean-Claude,
Briand Loïc
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.03.017
Subject(s) - chemistry , residue (chemistry) , biochemistry , mutagenesis , odorant binding protein , binding site , site directed mutagenesis , lipocalin , binding selectivity , stereochemistry , gene , mutation , mutant
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.