NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH.
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.
Lee
Donghan
D
Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule-Zürich, Zürich, Switzerland.
Damberger
Fred F
FF
Peng
Guihong
G
Horst
Reto
R
Güntert
Peter
P
Nikonova
Larisa
L
Leal
Walter S
WS
Wüthrich
Kurt
K
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
D002352:Carrier Proteins; D019476:Insect Proteins; D036341:Intercellular Signaling Peptides and Proteins; D008024:Ligands; C403094:pheromone-binding protein, Bombyx