title: NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH.
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.
authors.affiliation: Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule-Zürich, Zürich, Switzerland.
authors.forename: Donghan
authors.initials: D
authors.lastname: Lee
authors.forename: Fred F
authors.initials: FF
authors.lastname: Damberger
authors.forename: Guihong
authors.initials: G
authors.lastname: Peng
authors.forename: Reto
authors.initials: R
authors.lastname: Horst
authors.forename: Peter
authors.initials: P
authors.lastname: Güntert
authors.forename: Larisa
authors.initials: L
authors.lastname: Nikonova
authors.forename: Walter S
authors.initials: WS
authors.lastname: Leal
authors.forename: Kurt
authors.initials: K
authors.lastname: Wüthrich
mesh_terms: D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D057927:Hydrophobic and Hydrophilic Interactions; D019476:Insect Proteins; D036341:Intercellular Signaling Peptides and Proteins; D008024:Ligands; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary
chemical_list: D002352:Carrier Proteins; D019476:Insect Proteins; D036341:Intercellular Signaling Peptides and Proteins; D008024:Ligands; C403094:pheromone-binding protein, Bombyx