1znh
From Proteopedia
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|PDB= 1znh |SIZE=350|CAPTION= <scene name='initialview01'>1znh</scene>, resolution 2.1Å | |PDB= 1znh |SIZE=350|CAPTION= <scene name='initialview01'>1znh</scene>, resolution 2.1Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> | + | |LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=OC9:OCTAN-1-OL'>OC9</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= MUP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |GENE= MUP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1znd|1ZND]], [[1zng|1ZNG]], [[1zne|1ZNE]], [[1znk|1ZNK]], [[1znl|1ZNL]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1znh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1znh OCA], [http://www.ebi.ac.uk/pdbsum/1znh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1znh RCSB]</span> | ||
}} | }} | ||
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[[Category: Malham, R.]] | [[Category: Malham, R.]] | ||
[[Category: Phillips, S E.]] | [[Category: Phillips, S E.]] | ||
| - | [[Category: CD]] | ||
| - | [[Category: OC9]] | ||
[[Category: beta-barrel]] | [[Category: beta-barrel]] | ||
[[Category: lipocalin]] | [[Category: lipocalin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:39:10 2008'' |
Revision as of 22:39, 30 March 2008
| |||||||
| , resolution 2.1Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | MUP1 (Mus musculus) | ||||||
| Related: | 1ZND, 1ZNG, 1ZNE, 1ZNK, 1ZNL
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
1ZNH 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
Page seeded by OCA on Mon Mar 31 01:39:10 2008
