1ZNG
Strong Solute-Solute Dispersive Interactions in a Protein-Ligand Complex
Summary for 1ZNG
| Entry DOI | 10.2210/pdb1zng/pdb |
| Related | 1ZND 1ZNE 1ZNH 1ZNK 1ZNL |
| Descriptor | Major Urinary Protein, CADMIUM ION, HEPTAN-1-OL, ... (4 entities in total) |
| Functional Keywords | lipocalin, beta-barrel, transport protein |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Secreted: P11589 |
| Total number of polymer chains | 1 |
| Total formula weight | 20480.42 |
| Authors | Malham, R.,Johnstone, S.,Bingham, R.J.,Barratt, E.,Phillips, S.E.,Laughton, C.A.,Homans, S.W. (deposition date: 2005-05-11, release date: 2005-12-20, Last modification date: 2024-10-30) |
| Primary citation | 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 Cited by 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: 16316253DOI: 10.1021/ja055454g PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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