| Literature DB >> 12417333 |
Donghan Lee1, Fred F Damberger, Guihong Peng, Reto Horst, Peter Güntert, Larisa Nikonova, Walter S Leal, Kurt Wüthrich.
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.Entities:
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Year: 2002 PMID: 12417333 DOI: 10.1016/s0014-5793(02)03548-2
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124