J. Biol. Chem., Vol. 266, Issue 5, 2759-2762, Feb, 1991
Determination of alpha-subunit contact regions of human follicle- stimulating hormone beta-subunit using synthetic peptides
TA Santa-Coloma and LE Reichert Jr
Department of Biochemistry, Albany Medical College, New York 12208.
Follicle-stimulating hormone (FSH) is a glycoprotein hormone composed of
two different subunits designated FSH-alpha and FSH-beta. Using synthetic
peptides corresponding to the primary structure of human (h) FSH-beta
subunit, we previously identified two regions of the beta- subunit,
hFSH-(33-53) and hFSH-(81-95), as receptor binding regions. In this report,
we tested the ability of synthetic peptides to interact with
hFSH-alpha-subunit. Synthetic peptides corresponding to hFSH-beta- (11-25),
(41-55), (51-65), and (101-111) were able to bind specifically
radioiodinated hFSH-alpha-subunit, suggesting that they represent regions
of interaction with the alpha-subunit. These experimental results were in
agreement with the location of alpha-subunit contact regions predicted by
sequence analysis. Peptides of hFSH-beta-subunit showing maximum specific
binding to the alpha-subunit were those possessing minimum interaction with
receptor whereas those not binding to alpha-subunit corresponded to regions
shown to interact with receptor (hFSH-beta-(33-53) and hFSH-beta-(81-95].
The hFSH-beta- subunit, therefore, seems to have two discontinuous receptor
binding regions flanked by three alpha-subunit contact regions.
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