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

Donghan Lee; Fred F Damberger; Guihong Peng; Reto Horst; Peter Güntert; Larisa Nikonova; Walter S Leal; Kurt Wüthrich

doi:10.1016/s0014-5793(02)03548-2

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.

Authors

Donghan Lee¹, Fred F Damberger, Guihong Peng, Reto Horst, Peter Güntert, Larisa Nikonova, Walter S Leal, Kurt Wüthrich

Affiliation

¹ Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule-Zürich, Zürich, Switzerland.

PMID: 12417333
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