The structure, stability and pheromone binding of the male mouse protein sex pheromone darcin



Phelan, Marie M, McLean, Lynn, Armstrong, Stuart D ORCID: 0000-0002-3862-1801, Hurst, Jane L ORCID: 0000-0002-3728-9624, Beynon, Robert J ORCID: 0000-0003-0857-495X and Lian, Lu-Yun
(2014) The structure, stability and pheromone binding of the male mouse protein sex pheromone darcin. PLoS One, 9 (10).

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Abstract

Mouse urine contains highly polymorphic major urinary proteins that have multiple functions in scent communication through their abilities to bind, transport and release hydrophobic volatile pheromones. The mouse genome encodes for about 20 of these proteins and are classified, based on amino acid sequence similarity and tissue expression patterns, as either central or peripheral major urinary proteins. Darcin is a male specific peripheral major urinary protein and is distinctive in its role in inherent female attraction. A comparison of the structure and biophysical properties of darcin with MUP11, which belongs to the central class, highlights similarity in the overall structure between the two proteins. The thermodynamic stability, however, differs between the two proteins, with darcin being much more stable. Furthermore, the affinity of a small pheromone mimetic is higher for darcin, although darcin is more discriminatory, being unable to bind bulkier ligands. These attributes are due to the hydrophobic ligand binding cavity of darcin being smaller, caused by the presence of larger amino acid side chains. Thus, the physical and chemical characteristics of the binding cavity, together with its extreme stability, are consistent with darcin being able to exert its function after release into the environment.

Item Type: Article
Additional Information: ## TULIP Type: Electronic Journal ##
Depositing User: Symplectic Admin
Date Deposited: 13 Sep 2016 09:10
Last Modified: 10 Nov 2021 08:37
DOI: 10.1371/journal.pone.0108415
Open Access URL: http://journals.plos.org/plosone/article?id=10.137...
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URI: https://livrepository.liverpool.ac.uk/id/eprint/3003265