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. Author manuscript; available in PMC: 2015 Jul 8.
Published in final edited form as: Structure. 2014 Jun 5;22(7):961–973. doi: 10.1016/j.str.2014.04.013

Figure 1. Solution state conformational flexibility of full length PR-B.

Figure 1

Agonist (R5020) bound full length PR-B was analyzed by hydrogen deuterium exchange studies and the average % of deuterium incorporation across six different time points (0,10,30,60,300,900 and 3600 sec) is overlaid onto the crystal structure of PR LBD (PDB ID: 1A28) and PR DBD (PDB ID: 2C7A). The color is according to the color code at the bottom of the figure. The hinge region and N terminal domain are represented by schematics due to lack of atomic structure. Representative peptide deuterium build up curves from each domain are indicated at top.