1LS8
NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH
1LS8 の概要
| エントリーDOI | 10.2210/pdb1ls8/pdb |
| NMR情報 | BMRB: 6313 |
| 分子名称 | pheromone binding protein (1 entity in total) |
| 機能のキーワード | pheromone binding protein, bmpbp, bmpbpb, solution structure, transport protein |
| 由来する生物種 | Bombyx mori (domestic silkworm) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 15903.14 |
| 構造登録者 | Lee, D.,Damberger, F.,Horst, R.,Guntert, P.,Leal, W.S.,Wuthrich, K. (登録日: 2002-05-17, 公開日: 2002-11-20, 最終更新日: 2024-11-20) |
| 主引用文献 | Lee, 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: 12417333DOI: 10.1016/S0014-5793(02)03548-2 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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