Core structure of gp41 from the HIV envelope glycoprotein

Details Core structure of gp41 from the HIV envelope glycoprotein Core structure of gp41 from the HIV envelope glycoprotein

2008-07-22

2008-07-22

Campell, Bruce R. (Department: 1648)

Chemistry: molecular biology and microbiology

Measuring or testing process involving enzymes or...

Involving antigen-antibody binding, specific binding protein...

C435S005000

Reexamination Certificate

active

07402396

ABSTRACT:
Described are the crystal structure of the α-helical domain of the gp41 component of HIV-1 envelope glycoprotein which represents the core of fusion-active gp41, methods of identifying and designing drugs which inhibit gp41 function and drugs which do so.

REFERENCES:
patent: 5444044 (1995-08-01), Jiang et al.
patent: 5464933 (1995-11-01), Bolognesi et al.
patent: 5656480 (1997-08-01), Wild et al.
patent: 5780221 (1998-07-01), Schumacher et al.
patent: 5840843 (1998-11-01), Jiang et al.
patent: 6150088 (2000-11-01), Chan et al.
patent: 6506554 (2003-01-01), Chan et al.
patent: 6747126 (2004-06-01), Eckert et al.
patent: 6818740 (2004-11-01), Eckert et al.
patent: 6841657 (2005-01-01), Eckert et al.
patent: 7053179 (2006-05-01), Root et al.
patent: 7226598 (2007-06-01), Eckert et al.
patent: 2001/0047080 (2001-11-01), Root et al.
patent: 2002/0077284 (2002-06-01), Eckert et al.
patent: 2003/0082525 (2003-05-01), Root et al.
patent: 2003/0099935 (2003-05-01), Chan et al.
patent: 2004/0044183 (2004-03-01), Eckert et al.
patent: 2004/0213801 (2004-10-01), Wild et al.
patent: 2005/0221294 (2005-10-01), Eckert et al.
patent: 2006/0014139 (2006-01-01), Root et al.
patent: WO 94/02505 (1994-02-01), None
patent: WO 96/40191 (1996-12-01), None
patent: WO 98/32848 (1998-07-01), None
patent: WO 00/06599 (2000-02-01), None
patent: WO 00/40616 (2000-07-01), None
patent: WO 01/03723 (2001-01-01), None
patent: WO 01/44286 (2001-06-01), None
Baum, Rudy, “Virus-cell Fusion Targeted for Drug Development,” C&EN (1996).
Blacklow, Stephen C., et al., “A Trimeric Subdomain of the Simian Immunodeficiency Virus Envelope Glycoprotein,” Biochemistry, 34(46):14955-14962 (1995).
Blake, James and Li, Choh Hao, “Adrenocorticotropin. 47. Synthesis and Biological Activity of Adrenocorticotropic Peptides Modified at the Tryptophan Position,” J. Medicinal Chem. 18(4):423-426 (1975).
Borchardt, Allen et al., “Small Molecule-dependent genetic selection in stochastic nanodroplets as a means of detecting protein-ligand interactions on a large scale,” Chem. & Biol. 4(12):961-968 (1997).
Bullough, Per A. et al., “Structure of influenza haemagglutinin at the pH of membrane fusion,” Nature 371:37-43 (1994).
Caffrey, Michael et al., “Three-dimensional solution structure of the 44kDa ectodomain of SIV gp41,” EMBO J. 17(16):4572-4584 (1998).
Cao, Jie et al., “Effects of Amino Acid Changes in the Extracellular Domain of the Human Immunodeficiency Virus Type 1 gp41 Envelope Glycoprotein,” J. Virology 67(5):2747-2755 (1993).
Chabala, John C., “Solid-phase combinatorial chemistry and novel tagging methods for identifying leads,” Curr. Opin. Biotech. 6:632-639 (1995).
Chakrabartty, Avijit et al.,“Aromatic Side-Chain Contribution to Far-Ultraviolet Circular Dichroism of Helical Peptides and Its Effect on Measurement of Helix Propensities,” Biochemistry 32:5560-5565 (1993).
Chambers, Philip, et al., “Heptad Repeat Sequences are Located Adjacent to Hydrophobic Regions in Several Types of Virus Fusion Glycoproteins,” Journal of General Virology, 71:3075-3080 (1990).
Chan, David C., et al., “Evidence that a Prominent Cavity in the Coiled Coil of HIV Type I gp41 is an Attractive Drug Target,” Proc. Natl. Acad. Sci. USA 95:15613-15617 (1998).
Chan, David C., et al., “Core Structure of gp41 from the HIV Envelope Glycoprotein,” Cell 89:263-273 (1997).
Chan, David C. and Kim, Peter A., “HIV Entry and Its Inhibition,” Cell 93:681-684 (1998).
Chen, Yee-Hsiung et al., “Determination of the Helix and Form of Proteins in Aqueous Solution by Circular Dichroism,” Biochemistry 13(16):3350-3359 (1974).
Chen, Benjamin K. et al., “Distinct Modes of Human Immunodeficiency Virus Type 1 Proviral Latency Revealed by Superinfection of Nonproductively Infected Cell Lines with Recombinant Luciferase-Encoding Viruses,” J. Virology 68(2):654-660 (1994).
Chen, Charlie L. et al., “One Bead-One Compound Combinatorial Peptide Library: Different Types of Screening,” Methods in Enzymology 267:211-219 (1996).
Chen, Chin-Ho et al., “A Molecular Clasp in the Human Immunodeficiency Virus (HIV) Type 1 TM Protein Determines the Anti-HIV Activity of gp41 Derivatives:Implication for Viral Fusion,” J. Virology 69(6):3771-3777 (1995).
Cole, James L. and Garsky, Victor M., “Thermodynamics of Peptide Inhibitor Binding to HIV-1 gp41,” Biochemistry 40:5633-5641 (2001).
Delwart, Eric L., et al., “Retroviral Envelope Glycoproteins Contain a “Leucine Zipper”-like Repeat,” AIDS Research and Human Retroviruses, 6(6):703-706 (1990).
Doering Don S. and Matsudaira, Paul, “Cysteine Scanning Mutagenesis at 40 of 76 Positions in Villin Headpiece Maps the F-Actin Binding Site and Structuring Features of the Domain,” Biochemistry 35:12677-12685 (1996).
Dutch, Rebecca Ellis et al., “Paramyxovirus Fusion Protein: Characterization of the Core Trimer, a Rod-Shaper Complex with Helices in Anti-Parallel Orientation,” Virology 254:147-159 (1999).
Eckert, Debra M., et al., “Inhibiting HIV-1 Entry: Discovery of D-Peptide Inhibitors that Target the gp41 Coiled-Coil Pocket,” Cell 99:103-115 (1999).
Eckert, Debra M. et al., “Crystal Structure of GCN4-plQ1, a Trimeric Coiled Coil with Buried Polar Residues,” J. Mol. Biol. 284:859-865 (1998).
Eckhart, Leopold et al., “Immunogenic Presentation of a Conserved gp41 Epitope of Human Immunodeficiency Virus Type I on Recombinant Surface Antigen of Hepatitis B Virus,” J. Gen. Virol. 77:2001-2008 (1996).
Edelhoch, Harold, “Spectroscopic Determination of Trytophan and Tyrosine in Proteins,” Biochemistry 6:(7):1948-1954 (1967).
Fass, Deborah et al., “Retrovirus envelop domain at 1.7 resolution,” Nature Structural Biology 3(5):465-469 (1996).
Fass, Deborah and Kim, Peter S., “Dissection of a retrovirus envelope protein reveals structural similarity to influenza hemagglutinin,” Current Biology 5(12):1-7(1995).
Furuta et al., “Capture of an early fusion-active conformation of HIV-1 gp41,” Nature Structural Biology 5(4):276-279 (1998).
Gallaher, William R., et al., “A General Model for the Transmembrane Proteins of HIV and Other Retroviruses,” Aids Research and Human Retroviruses, 5(4):431-440 (1989).
Harbury, Pehr B. et al., “Repacking protein cores with backbone freedom:Structure prediction for coiled coils,” Proc. Natl. Acad. Sci, USA 92:8408-8412 (1995).
Harbury, Pehr B. et al., “Crystal structure of an isoleucine-zipper trimer,” Nature 371:80-83 (1994).
Hirsch, Vanessa M. and Johnson, Philip R., “Pathogenic diversity of simian immunodeficiency viruses,” Virus Research 32:183-206 (1994).
Hooft, Rob W.W. and Vriend, Gert, “Errors in protein structures,” Nature 381:272 (1996).
Jiang, Shibo et al., “A conformation-Specific Monoclonal Antibody Reacting with Fusion-Active gp41 from the Human Immunodeficiency Virus Type 1 Envelope Glycoprotein,” J. of Virology 72(12):10213-10217 (1998).
Jiang, S. et al., “A screening assay for antiviral compounds targeted to the HIV-1 gp41 core structure using a conformation-specific monoclonal antibody,” J. Virol. Methods 80:85-96 (1999).
Jiang, Shibo et al., “HIV-1 inhibition by a peptide,” Nature 365:113 (1993).
Jones, T.A. et al., “Improved Methods for Building Protein Models in Electron Density Maps and the Location of Errors in these Models,” Acta Cryst. A47:110-119 (1991).
Judice, J. Kevin et al., “Inhibition of HIV type 1 infectivity by constrained -helical peptides:Implications for the viral fusion mechanism,” Proc. Natl. Acad. Sci. USA 94:13426-13430 (1997).
Kilby, J. Michael et al., “Potent suppression of HIV-1 replication in humans by T-20, a peptide inhibitor of g

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