4.0 Article

H-1, N-15, and C-13 chemical shift assignments of the mosquito odorant binding protein-1 (CquiOBP1) bound to the mosquito oviposition pheromone

Journal

BIOMOLECULAR NMR ASSIGNMENTS
Volume 3, Issue 2, Pages 195-197

Publisher

SPRINGER
DOI: 10.1007/s12104-009-9173-5

Keywords

Odorant-binding protein; Pheromone signaling; Olfaction; NMR

Funding

  1. NIH [EY012347, 5U01AI058267-05]
  2. NSF [0234769]
  3. USDA-NRI [2003-35302-13648]
  4. Almond Board of California
  5. UC Davis NMR facility
  6. NATIONAL EYE INSTITUTE [R01EY012347] Funding Source: NIH RePORTER
  7. NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [U01AI058267] Funding Source: NIH RePORTER

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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 25A degrees C (BMRB no. 16175).

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