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1ls8
From Proteopedia
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[[Image:1ls8.gif|left|200px]] | [[Image:1ls8.gif|left|200px]] | ||
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'''NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH''' | '''NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH''' | ||
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[[Category: Lee, D.]] | [[Category: Lee, D.]] | ||
[[Category: Wuthrich, K.]] | [[Category: Wuthrich, K.]] | ||
| - | [[Category: | + | [[Category: Bmpbp]] |
| - | [[Category: | + | [[Category: Bmpbpb]] |
| - | [[Category: | + | [[Category: Nmr]] |
| - | [[Category: | + | [[Category: Pheromone binding protein]] |
| - | [[Category: | + | [[Category: Solution structure]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:14:10 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 21:14, 2 May 2008
NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH
Overview
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.
About this Structure
1LS8 is a Single protein structure of sequence from Bombyx mori. Full crystallographic information is available from OCA.
Reference
NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH., Lee D, Damberger FF, Peng G, Horst R, Guntert P, Nikonova L, Leal WS, Wuthrich K, FEBS Lett. 2002 Nov 6;531(2):314-8. PMID:12417333 Page seeded by OCA on Sat May 3 00:14:10 2008
