The goal of this proposal is to study the activation mechanism of the FSH receptor (FSH-R).
In Aim 1, the C-terminal residues of the FSH-a subunit will be examined to determine conclusively which amino acid(s) is involved in receptor activation, which might be involved in receptor binding, and what the structural and functional relationships of these amino acids are.
In Aim 2, the C-terminal half of the FSH-R will be investigated to identify the amino acid residues that are responsible for receptor activation and to determine their roles in receptor activation.
In Aim 3, the high affinity hormone contact points in the N-terminal half will be identified and the role of amino acids in hormone binding determined.

Agency
National Institute of Health (NIH)
Institute
National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
Type
Research Project (R01)
Project #
5R01DK051469-02
Application #
2518552
Study Section
Biochemical Endocrinology Study Section (BCE)
Program Officer
Sato, Sheryl M
Project Start
1996-09-15
Project End
2000-08-31
Budget Start
1997-09-26
Budget End
1998-08-31
Support Year
2
Fiscal Year
1997
Total Cost
Indirect Cost
Name
University of Wyoming
Department
Biochemistry
Type
Schools of Earth Sciences/Natur
DUNS #
069690956
City
Laramie
State
WY
Country
United States
Zip Code
82071
Ji, Inhae; Lee, ChangWoo; Jeoung, MyoungKun et al. (2004) Trans-activation of mutant follicle-stimulating hormone receptors selectively generates only one of two hormone signals. Mol Endocrinol 18:968-78
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Lee, ChangWoo; Ji, Inhae; Ryu, KiSung et al. (2002) Two defective heterozygous luteinizing hormone receptors can rescue hormone action. J Biol Chem 277:15795-800

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