(1)H, (15)N, and (13)C chemical shift assignments of the mosquito odorant binding protein-1 (CquiOBP1) bound to the mosquito oviposition pheromone.
An odorant-binding protein from the Southern house mosquito, Culex pipiens quinquefasciatus (Cqui-OBP1) binds to the mosquito oviposition pheromone (MOP), 6-acetoxy-5-hexadecanolide to facilitate the transport of MOP to membrane-bound odorant receptors. We report complete NMR chemical shift assignments of Cqui-OBP1 bound to the MOP pheromone obtained at pH 7.0 and 25 degrees C (BMRB no. 16175).
Xu
Xianzhong
X
Department of Chemistry, University of California, Davis, CA 95616, USA.
Xu
Wei
W
Ishida
Yuko
Y
Li
Yun
Y
Leal
Walter S
WS
Ames
James B
JB
D000818:Animals; D009033:Culicidae / Q000502:physiology; D006863:Hydrogen-Ion Concentration; D019476:Insect Proteins / Q000737:chemistry* / Q000378:metabolism*; D019906:Nuclear Magnetic Resonance, Biomolecular; D010058:Oviposition; D010675:Pheromones / Q000378:metabolism*; D018035:Receptors, Odorant / Q000737:chemistry* / Q000378:metabolism*
D019476:Insect Proteins; D010675:Pheromones; D018035:Receptors, Odorant; C045648:odorant-binding protein