Accueil > Publications > Recherche par années > Années 2000 > 2002

Lartigue, A ; Campanacci, V ; Roussel, A ; Larsson, AM ; Jones, TA ; Tegoni, M ; Cambillau, C

X-ray structure and ligand binding study of a moth chemosensory protein

Journal of Biological Chemistry 277 (35) 32094-32098

par Administrateur - publié le

Abstract :

Chemosensory proteins (CSPs) are believed to be involved in chemical communication and perception. Such proteins, of M-r 13,000, have been isolated from several sensory organs of a wide range of insect species. Several CSPs have been identified in the antennae and proboscis of the moth Mamestra brassicae. One of them, CSPMbraA6, a 112-amino acid antennal protein, has been expressed in large quantities and is soluble in the Escherichia coli periplasm. X-ray structure determination has been performed in parallel with ligand binding assays using tryptophan fluorescence quenching.