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To determine the location of a potential binding site for each receptor, we structurally aligned and superimposed each of the models onto the structures of bovine Rhodopsin ([[1l9h]], [[1f88]]), human β2-Adrenergic receptor ([[2rh1]]) and human A2-Adenosine receptor ([[3eml]]). The Prokineticin receptors binding sites were determined based on homology to the known binding site-composing residues of the templates.
To determine the location of a potential binding site for each receptor, we structurally aligned and superimposed each of the models onto the structures of bovine Rhodopsin ([[1l9h]], [[1f88]]), human β2-Adrenergic receptor ([[2rh1]]) and human A2-Adenosine receptor ([[3eml]]). The Prokineticin receptors binding sites were determined based on homology to the known binding site-composing residues of the templates.


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For more information on our group, please visit us at [http://departments.agri.huji.ac.il/biochemfoodsci722/teachers/niv_masha/index.htm. HUJI].
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