3DXL
Crystal structure of AeD7 from Aedes Aegypti
3DXL の概要
エントリーDOI | 10.2210/pdb3dxl/pdb |
分子名称 | Allergen Aed a 2, CHLORIDE ION, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (5 entities in total) |
機能のキーワード | odorant-binding protein, all-helical, allergen, secreted |
由来する生物種 | Aedes aegypti (Yellowfever mosquito) |
細胞内の位置 | Secreted : P18153 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 35643.82 |
構造登録者 | Andersen, J.F.,Calvo, E.,Mans, B.J.,Ribeiro, J.M. (登録日: 2008-07-24, 公開日: 2009-02-03, 最終更新日: 2021-03-31) |
主引用文献 | Calvo, E.,Mans, B.J.,Ribeiro, J.M.,Andersen, J.F. Multifunctionality and mechanism of ligand binding in a mosquito antiinflammatory protein Proc.Natl.Acad.Sci.USA, 106:3728-3733, 2009 Cited by PubMed Abstract: The mosquito D7 salivary proteins are encoded by a multigene family related to the arthropod odorant-binding protein (OBP) superfamily. Forms having either one or two OBP domains are found in mosquito saliva. Four single-domain and one two-domain D7 proteins from Anopheles gambiae and Aedes aegypti (AeD7), respectively, were shown to bind biogenic amines with high affinity and with a stoichiometry of one ligand per protein molecule. Sequence comparisons indicated that only the C-terminal domain of AeD7 is homologous to the single-domain proteins from A. gambiae, suggesting that the N-terminal domain may bind a different class of ligands. Here, we describe the 3D structure of AeD7 and examine the ligand-binding characteristics of the N- and C-terminal domains. Isothermal titration calorimetry and ligand complex crystal structures show that the N-terminal domain binds cysteinyl leukotrienes (cysLTs) with high affinities (50-60 nM) whereas the C-terminal domain binds biogenic amines. The lipid chain of the cysLT binds in a hydrophobic pocket of the N-terminal domain, whereas binding of norepinephrine leads to an ordering of the C-terminal portion of the C-terminal domain into an alpha-helix that, along with rotations of Arg-176 and Glu-268 side chains, acts to bury the bound ligand. PubMed: 19234127DOI: 10.1073/pnas.0813190106 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.3 Å) |
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