| Title: | NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH |
| Author(s): | Lee D; Damberger FF; Peng G; Horst R; Guntert P; Nikonova L; Leal WS; Wuthrich K; |
| Address: | "Institut fur Molekularbiologie und Biophysik, Eidgenossische Technische Hochschule-Zurich, Zurich, Switzerland" |
| DOI: | 10.1016/s0014-5793(02)03548-2 |
| ISSN/ISBN: | 0014-5793 (Print) 0014-5793 (Linking) |
| 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" |
| Keywords: | "Carrier Proteins/*chemistry/metabolism Hydrogen-Ion Concentration Hydrophobic and Hydrophilic Interactions *Insect Proteins Intercellular Signaling Peptides and Proteins Ligands *Models, Molecular Nuclear Magnetic Resonance, Biomolecular Protein Structure;" |
| Notes: | "MedlineLee, Donghan Damberger, Fred F Peng, Guihong Horst, Reto Guntert, Peter Nikonova, Larisa Leal, Walter S Wuthrich, Kurt eng Research Support, Non-U.S. Gov't England 2002/11/06 FEBS Lett. 2002 Nov 6; 531(2):314-8. doi: 10.1016/s0014-5793(02)03548-2" |
