1LS8

NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH

Summary for 1LS8

• Entry DOI: 10.2210/pdb1ls8/pdb
• NMR Information: BMRB: 6313
• Descriptor: pheromone binding protein (1 entity in total)
• Functional Keywords: pheromone binding protein, bmpbp, bmpbpb, solution structure, transport protein
• Biological source: Bombyx mori (domestic silkworm)
• Total number of polymer chains: 1
• Total formula weight: 15903.14

Authors

Lee, D.,Damberger, F.,Horst, R.,Guntert, P.,Leal, W.S.,Wuthrich, K. (deposition date: 2002-05-17, release date: 2002-11-20, Last modification date: 2022-02-23)

Primary citation

Lee, D.,Damberger, F.F.,Horst, R.,Guntert, P.,Nikonova, L.,Leal, W.S.,Wuthrich, K.
NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH
FEBS Lett., 531:314-318, 2002

PubMed Abstract: The nuclear magnetic resonance structure of the unliganded pheromone-binding protein (PBP) from Bombyx mori at pH above 6.5, BmPBP(B), consists of seven helices with residues 3-8, 16-22, 29-32, 46-59, 70-79, 84-100, and 107-124, and contains the three disulfide bridges 19-54, 50-108, and 97-117. This polypeptide fold encloses a large hydrophobic cavity, with a sufficient volume to accommodate the natural ligand bombykol. The polypeptide folds in free BmPBP(B) and in crystals of a BmPBP-bombykol complex are nearly identical, indicating that the B-form of BmPBP in solution represents the active conformation for ligand binding.

PubMed: 12417333
DOI: 10.1016/S0014-5793(02)03548-2

Experimental method

SOLUTION NMR