Water soluble g-protein coupled receptor
AssigneeThe Trustees of the University of Pennsylvania
InventorsRenyu LIU, Jeffery G. SAVEN, Jose Manuel PEREZ-AGUILAR, Felipe MATSUNAGA, Jin XI
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Abstract
Described herein are recombinant integral membrane proteins having multiple transmembrane domains that have been engineered to be less hydrophobic, through alteration of the amino acid sequence of the native protein, but retain the ability to bind their natural ligand. The decreased hydrophobicity of the described proteins makes them more water soluble than the native protein, which allows the described proteins to be expressed in bacteria in large quantities and isolated in the absence of membranes, all while retaining the ability to interact with known ligands.
Claims24
A recombinant integral membrane protein having seven transmembrane domains, comprising 4 transmembrane domains each having at least 3 amino acid mutations that decrease the overall hydrophobicity of the recombinant integral membrane protein relative to that of the native protein.
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A polynucleotide encoding a recombinant integral membrane protein having seven transmembrane domains, comprising 4 transmembrane domains each having at least 3 amino acid mutations that decrease the overall hydrophobicity of the recombinant integral membrane protein relative to that of the native protein.
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A method of identifying a binding compound for a recombinant integral membrane protein having seven transmembrane domains, comprising 4 transmembrane domains each having at least 3 amino acid mutations that decrease the overall hydrophobicity of the recombinant integral membrane protein relative to that of the native protein, comprising contacting said recombinant integral membrane protein with a compound and determining the affinity of said recombinant integral membrane protein for said compound.
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Dependencies are inferred from the claim text.