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1LS8

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

Summary for 1LS8
Entry DOI10.2210/pdb1ls8/pdb
NMR InformationBMRB: 6313
Descriptorpheromone binding protein (1 entity in total)
Functional Keywordspheromone binding protein, bmpbp, bmpbpb, solution structure, transport protein
Biological sourceBombyx mori (domestic silkworm)
Total number of polymer chains1
Total formula weight15903.14
Authors
Lee, D.,Damberger, F.,Horst, R.,Guntert, P.,Leal, W.S.,Wuthrich, K. (deposition date: 2002-05-17, release date: 2002-11-20, Last modification date: 2024-11-20)
Primary citationLee, D.,Damberger, F.F.,Horst, R.,Guntert, P.,Nikonova, L.,Leal, W.S.,Wuthrich, K.
NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH
FEBS Lett., 531:314-318, 2002
Cited by
PubMed 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.
PubMed: 12417333
DOI: 10.1016/S0014-5793(02)03548-2
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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数据于2025-07-09公开中

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