Millisecond activation switch for seven-transmembrane proteins

Details Millisecond activation switch for seven-transmembrane proteins Millisecond activation switch for seven-transmembrane proteins

2003-12-19

2011-12-27

Pak, Michael (Department: 1646)

Chemistry: natural resins or derivatives; peptides or proteins;

Proteins, i.e., more than 100 amino acid residues

Reexamination Certificate

active

08084575

ABSTRACT:
The present invention relates to recombinant seven-transmembrane receptor, whereby the amino terminus of said recombinant receptor is located on an extracellular side and the carboxy-terminus is located on an intracellular side of a membrane, comprising at least two detectable labels, whereby a first of said at least two detectable labels is or is located on the carboxy-terminus and whereby a second of said at least two labels is or is located on the first or third intracellular loop or whereby a first of said at least two labels is or is located on the third intracellular loop. Furthermore, nucleic acid molecules encoding said recombinant seven-transmembrane receptors are described as well as vector and host cells comprising the same. Furthermore, the present invention provides for identification and screening methods for molecules or compounds which are capable of modifying the biological end of pharmacological function of seven-transmembrane receptor proteins. Finally, diagnostic compositions comprising the compounds of the present invention as well as kits comprising said compounds are disclosed.

REFERENCES:
patent: 6197534 (2001-03-01), Lakowicz et al.
patent: 6277627 (2001-08-01), Hellinga
patent: 2002/0048811 (2002-04-01), Devreotes et al.
patent: WO 98/40477 (1998-09-01), None
patent: WO 99/66324 (1999-12-01), None
patent: WO 00/34318 (2000-06-01), None
patent: WO 01/09328 (2001-02-01), None
Altenbach et al., “Structure and function in rhodopsin: mapping light-dependent changes in distance between residue 316 in helix 8 and residues in the sequence 60-75, covering the cytoplasmic end of helices TM1 and TM2 and their connection loop CL1,”Biochemistry, 40:15493-15500, 2001.
Angers et al., “Detection of beta 2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET),”Proc. Natl. Acad. Sci. USA, 97:3684-3689, 2000.
Angers et al., “Dimerization: an emerging concept for G protein-coupled receptor ontogeny and function,”Annu. Rev. Pharamacol. Toxicol., 42:409-435, 2002.
Baird et al., “Circular permutation and receptor insertion within green fluorescent proteins,”Proc. Natl. Acad. Sci. USA, 96:11241-11246, 1999.
Babcock et al., “Ligand-independent dimerization of CXCR4, a principal HIV-1 coreceptor,”J. Biol. Chem., 278:3378-3385, 2003.
Bourne and Meng, “Structure: Rhodopsin Sees the Light,”Science, 289:733-734, 2000.
Bunemann et al., “Activation and deactivation kinetics of alpha 2A- and alpha 2C-adrenergic receptor-activated G protein-activated inwardly rectifying K+ channel currents,”J. Biol. Chem., 276:47512-47517, 2001.
Chang and Weiss, “Site-specific fluorescence reveals distinct structural changes with GABA receptor activation and antagonism,”Nature Neurosci., 5:1163-1168, 2002.
Gaietta et al., “Multicolor and Electron Microscopic Imaging of Connexin Trafficking,”Science, 296:503-507, 2002.
Gardella and Juppner, “Molecular properties of the PTH/PTHrP receptor,”Trends Endocrinol. Metabolism, 12:210-217, 2001.
GenBank accession No. M97370, Dec. 31, 1994.
GenBank accession No. M99377, Apr. 27, 1993.
GenBank accession No. NM—011199, Nov. 17, 2006.
GenBank accession No. U22401, Sep. 20, 2001.
GenBank accession No. NM—000681, Nov. 17, 2006.
Gether, “Uncovering molecular mechanisms involved in activation of G protein-coupled receptors,”Endocr. Rev., 21:90-113, 2000.
Gether et al., “Fluorescent labeling of purified beta 2 adrenergic receptor. Evidence for ligand-specific conformational changes,”J. Biol. Chem., 270:28268-28275, 1995.
Ghanouni et al., “Functionally different agonists induce distinct conformations in the G protein coupling domain of the beta 2 adrenergic receptor,”J. Biol. Chem., 276:24433-24436, 2001.
Ghanouni et al, “Agonist-induced conformational changes in the G-protein-coupling domain of the beta 2 adrenergic receptor,”Proc. Natl. Acad. Sci. USA, 98:5997-6002, 2001.
Griesbeck et al., “Reducing the environmental sensitivity of yellow fluorescent protein. Mechanism and applications,”J. Biol. Chem., 276:29188-29194, 2001.
Griffin et al., “Specific Covalent Labeling of Recombinant Protein Molecules Inside Live Cells,”Science, 281:269-272, 1998.
Heikal et al., “Molecular spectroscopy and dynamics of intrinsically fluorescent proteins: coral red (dsRed) and yellow (Citrine),”Proc. Natl. Acad. Sci. USA, 97:11996-12001, 2000.
Heim, “Green fluorescent protein forms for energy transfer,”Methods Enzymol., 302:408-423, 1999.
Honda et al., “Spatiotemporal dynamics of guanosine 3′,5′-cyclic monophosphate revealed by a genetically encoded, fluorescent indicator,”Proc. Natl. Acad. Sci. USA, 98:2437-2442, 2001.
Huang et al., “The N-terminal region of the third intracellular loop of the parathyroid hormone (PTH)/PTH-related peptide receptor is critical for coupling to cAMP and inositol phosphate/Ca2+ signal transduction pathways,”J. Biol. Chem., 271:33382-33389, 1996.
Illes et al., “Signaling by extracellular nucleotides and nucleosides,”Naunyn-Schmiedebergs Arch. Pharmacol., 362:295-298, 2000.
Jensen et al., “Agonist-induced conformational changes at the cytoplasmic side of transmembrane segment 6 in the beta 2 adrenergic receptor mapped by site-selective fluorescent labeling,”J. Biol. Chem., 276:9279-9290, 2001.
Karatani et al., “Properties of the bimodal fluorescent protein produced byPhotobacterium phosphoreum,” Photochem. Photobiol., 71:230-236, 2000.
Kobilka and Gether, “Use of fluorescence spectroscopy to study conformational changes in the beta 2-adrenoceptor,”Methods Enzymol., 343:170-182, 2002.
Lim and Neubig, “Selective inactivation of guanine-nucleotide-binding regulatory protein (G-protein) alpha and betagamma subunits by urea,”Biochem. J., 354:337-344, 2001.
Loshe et al., “Direct optical recording of intrinsic efficacy at a G protein-coupled receptor,”Life Sciences, 74: 397-404, 2003.
Mercier et al., “Quantitative assessment of beta 1- and beta 2-adrenergic receptor homo- and heterodimerization by bioluminescence resonance energy transfer,”J. Biol. Chem., 277:44925-44931, 2002.
Milligan, “Strategies to identify ligands for orphan G-protein-coupled receptors,”Biochemical Society Transactions, 30:789-793, 2002.
Okada et al., “Activation of rhodopsin: new insights from structural and biochemical studies,”Trends Biochem. Sci., 26:318-324, 2001.
Pierce et al., “Seven-transmembrane receptors,”Nat. Rev. Mol. Cell Biol., 3:639-650, 2002.
Prasher et al., “Primary structure of theAequorea victoriagreen-fluorescent protein,”Gene, 111:229-233, 1992.
Rios et al., “G-protein-coupled receptor dimerization: modulation of receptor function,”Pharmacol. Ther., 92:71-87, 2001.
Sheikh et al., “Similar structures and shared switch mechanisms of the beta2-adrenoceptor and the parathyroid hormone receptor. Zn(II) bridges between helices III and VI block activation,”J. Biol. Chem., 274: 17033-17041, 1999.
Teller et al., “Advances in Determination of a High-Resolution Three-Dimensional Structure of Rhodopsin, A Model of G-Protein-Coupled Receptors(GPCRs),”Biochemistry, 40:7768-7772, 2001.
Strange, “Mechanisms of inverse agonism at G-protein-coupled receptors,”Trends Pharmocol Sci., 23:89-95, 2002.
Tsien, “The green fluorescent protein,”Ann. Rev. Biochem., 67:509-544, 1998.
Vilardaga et al., “Measurement of the millisecond activation switch of G protein-coupled receptors in living cells,”Nature Biotechnology, 21:807-812, 2003.

Affiliated with

Also associated with

Rating

Millisecond activation switch for seven-transmembrane proteins does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Millisecond activation switch for seven-transmembrane proteins, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Millisecond activation switch for seven-transmembrane proteins will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-4313637