Structural highlights
Function
MUP2_MOUSE Binds pheromones that are released from drying urine of males. These pheromones affect the sexual behavior of females.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Malham R, Johnstone S, Bingham RJ, Barratt E, Phillips SE, Laughton CA, Homans SW. Strong solute-solute dispersive interactions in a protein-ligand complex. J Am Chem Soc. 2005 Dec 7;127(48):17061-7. PMID:16316253 doi:10.1021/ja055454g
