The solution NMR structure of Antheraea polyphemus PBP provides new insight into pheromone recognition by pheromone-binding proteins;Erratum: The solution NMR structure of Antheraea polyphemus PBP provides new insight into pheromone recognition by pheromone-binding proteins (Journal of Molecular Biology (2004) 337 (443-451) DOI: 10.1016/j.jmb.2004.01.009)

Journal of Molecular Biology

Volumn 338, Issue 5, 2004, Pages 1037-

  Mohanty, Smita ^a   Zubkov, Sergey ^a   Gronenborn, Angela M ^b  

^a STONY BROOK UNIVERSITY   (United States)

^b NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

Author keywords

Antheraea polyphemus; ApolPBP, Antheraea polyphemus PBP; GOBP, general OBP; GPCR, G protein coupled receptor; NMR structure; OBP, odorant binding protein; Olfaction; PBP; PBP, pheromone binding protein; Pheromone binding protein

Indexed keywords

ERRATUM; PRIORITY JOURNAL; RETRACTED ARTICLE;

ANTHERAEA; ANTHERAEA POLYPHEMUS; POLYPHEMUS;

EID: 2142695719     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.01.009     Document Type: Article

References (3)

1. Wojtasek H., Leal W.S. Conformational change in the pheromone-binding protein from Bombyx mori induced by pH and by interaction with membranes. J. Biol. Chem. 274:1999;30950-30956
2. Damberger F., Nikonova L., Horst R., Peng G., Leal W.S., Wüthrich K. NMR characterization of a pH-dependent equilibrium between two folded solution conformations of the pheromone-binding protein from Bombyx mori. Protein Sci. 9:2000;1038-1041
3. Horst R., Damberger F., Luginbühl P., Güntert P., Peng G., Nikonova L., et al. NMR structure reveals intramolecular regulation mechanism for pheromone binding and release. Proc. Natl Acad. Sci. USA. 98:2001;14374-14379