NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH.
- Lee D Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule-Zürich, Zürich, Switzerland.
- Damberger FF
- Peng G
- Horst R
- Güntert P
- Nikonova L
- Leal WS
- Wüthrich K
- 2002-11-06
Published in:
- FEBS letters. - 2002
Carrier Proteins
Hydrogen-Ion Concentration
Hydrophobic and Hydrophilic Interactions
Insect Proteins
Intercellular Signaling Peptides and Proteins
Ligands
Models, Molecular
Nuclear Magnetic Resonance, Biomolecular
Protein Structure, Secondary
English
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.
- Language
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- English
- Open access status
- bronze
- Identifiers
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- DOI 10.1016/s0014-5793(02)03548-2
- PMID 12417333
- Persistent URL
- https://folia.unifr.ch/global/documents/71525
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