@article {20433,
	title = {3D models of lamprey progesterone receptor complexed with progesterone, 7alpha-hydroxy-progesterone and 15alpha-hydroxy-progesterone},
	journal = {Steroids},
	volume = {76},
	number = {1-2},
	year = {2011},
	note = {<p>Steroids. 2011 Jan;76(1-2):169-76. doi: 10.1016/j.steroids.2010.10.008. Epub 2010 Nov 3.</p>},
	month = {Jan},
	pages = {169-76},
	edition = {2010/11/09},
	abstract = {<p>Sea lamprey, a basal vertebrate, contains a progesterone receptor [PR]. An unusual property of lamprey is that gonadotropin-releasing hormone induces synthesis of 15alpha-hydroxy-progesterone [15alpha-OH-P] instead of progesterone. There also is indirect evidence for 7alpha-OH-P in lamprey serum. To determine if there is a structural basis for the binding of 7alpha-OH-P and 15alpha-OH-P to lamprey PR, we constructed 3D models of the lamprey PR complexed with progesterone, 7alpha-OH-P and 15alpha-OH-P. These 3D models reveal that Met-277 in lamprey PR has a specific interaction with the 15alpha-hydroxyl on 15alpha-OH-P and with Met-192, which also contacts the 15alpha-hydroxyl group. We also find that 7alpha-OH-P has favorable contacts with side-chains in lamprey PR. BLAST searches reveal that Met-277 on lamprey PR is unique among vertebrate PRs. This unique site on lamprey PR could be a target for compounds to control reproduction in sea lamprey, an environmental pest in Lake Michigan.</p>},
	keywords = {\&, Amino Acid Sequence, Animals, derivatives/ chemistry, Humans, Lampreys, Models, Molecular, Molecular Sequence Data, Progesterone/ analogs, Progesterone/ chemistry, Receptors, Sequence Alignment},
	isbn = {1878-5867 (Electronic)00},
	author = {Baker, M. E. and Asnaashari, P. and Chang, D. J. and McDonnell, S.}
}
