The binding cavity of mouse major urinary protein is optimised for a variety of ligand binding modes.
By T. Pertinhez, E. Ferrari, E. Casali, J. A. Patel, A. Spisni, Lorna J. Smith. 2009
22 citations recorded by the source corpus.
Subfields: Molecular Biology, Spectroscopy
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- Jane Hurst
- M. Phelan
- R. Beynon
- L. McLean
- S. Armstrong
- L. Lian
Citations in the corpus
- The Structure, Stability and Pheromone Binding of the Male Mouse Protein Sex Pheromone Darcin (2014, result): “The favourable enthalpy results from the binding of the SBT in the cavity rather than to a greater loss of degrees of freedom in protein upon binding; this is supported by evidence from structural studies for other MUPs where there appears to be only minimal changes in protein conformation upon pher”