1ZND

Strong Solute-Solute Dispersive Interactions in a Protein-Ligand Complex

1ZND の概要

• エントリーDOI: 10.2210/pdb1znd/pdb
• 関連するPDBエントリー: 1ZNE 1ZNG 1ZNH 1ZNK 1ZNL
• 分子名称: Major Urinary Protein, CADMIUM ION, PENTAN-1-OL, ... (4 entities in total)
• 機能のキーワード: lipocalin, beta-barrel, transport protein
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Secreted: P11589
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20540.52

構造登録者

Malham, R.,Johnstone, S.,Bingham, R.J.,Barratt, E.,Phillips, S.E.,Laughton, C.A.,Homans, S.W. (登録日: 2005-05-11, 公開日: 2005-12-20, 最終更新日: 2023-08-23)

主引用文献

Malham, R.,Johnstone, S.,Bingham, R.J.,Barratt, E.,Phillips, S.E.,Laughton, C.A.,Homans, S.W.
Strong Solute-Solute Dispersive Interactions in a Protein-Ligand Complex.
J.Am.Chem.Soc., 127:17061-17067, 2005

PubMed Abstract: The contributions of solute-solute dispersion interactions to binding thermodynamics have generally been thought to be small, due to the surmised equality between solute-solvent dispersion interactions prior to the interaction versus solute-solute dispersion interactions following the interaction. The thermodynamics of binding of primary alcohols to the major urinary protein (MUP-I) indicate that this general assumption is not justified. The enthalpy of binding becomes more favorable with increasing chain length, whereas the entropy of binding becomes less favorable, both parameters showing a linear dependence. Despite the hydrophobicity of the interacting species, these data show that binding is not dominated by the classical hydrophobic effect, but can be attributed to favorable ligand-protein dispersion interactions.

PubMed: 16316253
DOI: 10.1021/ja055454g

実験手法

X-RAY DIFFRACTION (1.6 Å)