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Vol. 53, Issue 2, 234-240, February 1998
Merck Research Laboratories, Rahway, New Jersey 07065 (T.M.F.,
R.-R.C.H, M.R.T, C.M., T.S., J.V., L.H.T.V.d.P.), and
Department of
Anatomy and Neurobiology, Washington University School of Medicine, St.
Louis, Missouri 63110 (V.V.K., J.E.K)
The leptin receptor is a member of the class I cytokine receptor family
and is involved in the control of appetite and body weight. The
predicted amino acid sequence of the extracellular region of the cloned
leptin receptor differs from that of many other cytokine receptors in
that it contains two homologous segments representing potential ligand
binding sites. After the analysis of various deletion and substitution
mutants of the leptin receptor, we found that the first potential
binding motif is not required for leptin binding and receptor
activation, whereas modification of the second potential binding motif
can lead to inactive receptor mutants. Further deletion analysis
generated a minimal binding domain that retains high affinity leptin
binding. The leptin binding domain thus has been localized to residues
323-640, which contain the second segment of cytokine receptor
domain/fibronectin type 3 domain (residues 428-635). Coexpression of
the active isoform of leptin receptor (OB-Rb) with an inactive mutant
lacking high affinity leptin binding site led to suppression of the
activity mediated by OB-Rb, suggesting that the leptin receptor may
exist as a multimeric complex in the absence of leptin.
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