LINDSEY JUNE BOWMAN, PHARM.D.
Pharmacy at Zion Ave, San Diego, CA
License number
California 61465
Category
Pharmacy
Type
Pharmacist
Address
Address
4647 Zion Ave, San Diego, CA 92120
Phone
(619) 528-6082
Personal information
See more information about LINDSEY JUNE BOWMAN at radaris.comName
Address
Phone
10034 Riverhead Dr, San Diego, CA 92129
2860 Doidge Ave, Pinole, CA 94564
11822 Still Rd, Grass Valley, CA 95949
2409 Turk Blvd, San Francisco, CA 94118
45861 Verba Santa Dr, Palm Desert, CA 92260
Professional information
Structure Of The Farnesoid X Receptor Ligand Binding Domain And Methods Of Use Therefor
US Patent:
2006019, Aug 31, 2006
Filed:
Nov 14, 2003
Appl. No.:
10/535042
Inventors:
Michael Downes - San Diego CA, US
Mark Verdicia - New York NY, US
Joseph Noel - San Diego CA, US
Ronald Evans - La Jolla CA, US
Lindsey Bowman - San Diego CA, US
Marianne Bowman - San Diego CA, US
Mark Verdicia - New York NY, US
Joseph Noel - San Diego CA, US
Ronald Evans - La Jolla CA, US
Lindsey Bowman - San Diego CA, US
Marianne Bowman - San Diego CA, US
International Classification:
G06F 19/00, C07K 14/705
US Classification:
530350000, 702019000
Abstract:
The present invention provides compositions comprising the ligand binding domain (LBD) of a farnesoid X receptor (FXR) in crystalline form. In alternative embodiments, the LBD of FXR is complexed with a ligand therefor. There are provided high resolution structures of FXR complexed with a novel high affinity agonist, fexaramine. The discovered structure of a FXR LBD provides the first three-dimensional view of the structural basis for FXR ligand binding. The present invention further provides a computer for producing a three-dimensional representation of FXR or a complex thereof, and a computer for determining at least a portion of the structure coordinates of FXR or a complex thereof. The present invention further provides methods of using this structural information to predict molecules capable of binding to FXR; to identify compounds with agonist, antagonist or partial agonist activity for FXR; and to determine whether a test compound is capable of binding to the LBD of FXR. The present invention further provides compositions comprising compounds identified by such invention methods.
Structure Of The Farnesoid X Receptor Ligand Binding Domain And Methods Of Use Therefor
US Patent:
8212006, Jul 3, 2012
Filed:
Jan 12, 2010
Appl. No.:
12/686347
Inventors:
Michael R. Downes - San Diego CA, US
Mark A. Verdicia - New York NY, US
Joseph P. Noel - San Diego CA, US
Ronald M. Evans - La Jolla CA, US
Lindsey J. Bowman - San Diego CA, US
Marianne Bowman - San Diego CA, US
Mark A. Verdicia - New York NY, US
Joseph P. Noel - San Diego CA, US
Ronald M. Evans - La Jolla CA, US
Lindsey J. Bowman - San Diego CA, US
Marianne Bowman - San Diego CA, US
Assignee:
The Salk Institute for Biological Studies - La Jolla CA
International Classification:
C07K 1/00, G06G 7/58, A01N 61/00
US Classification:
530350, 703 11, 514 1
Abstract:
The present invention provides compositions comprising the ligand binding domain (LBD) of a farnesoid X receptor (FXR) in crystalline form. In alternative embodiments, the LBD of FXR is complexed with a ligand therefor. There are provided high resolution structures of FXR complexed with a novel high affinity agonist fexaramine. The discovered structure of a FXR LBD provides the first three-dimensional view of the structural basis for FXR ligand binding. The present invention further provides a computer for producing a time-dimensional representation of FXR or a complex thereof, and a computer for determining at least a portion of the structure coordinates of FXR or a complex thereof. The present invention further provides methods of using this structural information to predict molecules capable of binding to FXR; to identify compounds with agonist, antagonist or partial agonist activity for FXR; and to determine whether a test compound is capable of binding to the LBD of FXR. The present invention further provides compositions comprising compounds identified by such invention methods.