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

FEBS Lett. 2002 Nov 6;531(2):314-8. doi: 10.1016/s0014-5793(02)03548-2.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carrier Proteins / chemistry*
  • Carrier Proteins / metabolism
  • Hydrogen-Ion Concentration
  • Hydrophobic and Hydrophilic Interactions
  • Insect Proteins*
  • Intercellular Signaling Peptides and Proteins
  • Ligands
  • Models, Molecular*
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Structure, Secondary

Substances

  • Carrier Proteins
  • Insect Proteins
  • Intercellular Signaling Peptides and Proteins
  • Ligands
  • pheromone-binding protein, Bombyx