1znl: Difference between revisions
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[[Image:1znl.gif|left|200px]] | [[Image:1znl.gif|left|200px]] | ||
'''Strong Solute-Solute Dispersive Interactions in a Protein-Ligand Complex''' | {{Structure | ||
|PDB= 1znl |SIZE=350|CAPTION= <scene name='initialview01'>1znl</scene>, resolution 1.7Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> and <scene name='pdbligand=DE1:DECAN-1-OL'>DE1</scene> | |||
|ACTIVITY= | |||
|GENE= MUP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |||
}} | |||
'''Strong Solute-Solute Dispersive Interactions in a Protein-Ligand Complex''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1ZNL is a [ | 1ZNL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZNL OCA]. | ||
==Reference== | ==Reference== | ||
Strong solute-solute dispersive interactions in a protein-ligand complex., Malham R, Johnstone S, Bingham RJ, Barratt E, Phillips SE, Laughton CA, Homans SW, J Am Chem Soc. 2005 Dec 7;127(48):17061-7. PMID:[http:// | Strong solute-solute dispersive interactions in a protein-ligand complex., Malham R, Johnstone S, Bingham RJ, Barratt E, Phillips SE, Laughton CA, Homans SW, J Am Chem Soc. 2005 Dec 7;127(48):17061-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16316253 16316253] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: lipocalin]] | [[Category: lipocalin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:37:44 2008'' | ||
Revision as of 13:37, 20 March 2008
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| 1znl, resolution 1.7Å | |||||||||||||
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| Ligands: | CD and DE1 | ||||||||||||
| Gene: | MUP1 (Mus musculus) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Strong Solute-Solute Dispersive Interactions in a Protein-Ligand Complex
Overview
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.
About this Structure
1ZNL is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Strong solute-solute dispersive interactions in a protein-ligand complex., Malham R, Johnstone S, Bingham RJ, Barratt E, Phillips SE, Laughton CA, Homans SW, J Am Chem Soc. 2005 Dec 7;127(48):17061-7. PMID:16316253
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